J. Stubbe

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Convergent allostery in ribonucleotide reductase

James Z. Chen, J. Bacik, W. Thomas, 2018, Nature Communications.

Christian Raetz: scientist and friend extraordinaire.

H. Nikaido, J. Stubbe, W. Wickner, 2013, Annual review of biochemistry.

Tangled up in knots: structures of inactivated forms of E. coli class Ia ribonucleotide reductase.

F. Asturias, E. Brignole, N. Ando, 2012, Structure.

UV Endonuclease V from Bacteriophage T4 Catalyzes DNA Strand Cleavage at Aldehydic Abasic Sites by a Syn β-Elimination Reaction

J. Gerlt, M. Absalon, J. Stubbe, 1989 .

Transcriptional analysis of Ralstonia eutropha genes related to poly-(R)-3-hydroxybutyrate homeostasis during batch fermentation

A. Sinskey, J. Stubbe, Pinghua Liu, 2005, Applied Microbiology and Biotechnology.

Purification and characterization of the purE, purK, and purC gene products: identification of a previously unrecognized energy requirement in the purine biosynthetic pathway.

J. Stubbe, J. Smith, B. Bhat, 1992, Biochemistry.

Synthesis, characterization and solution structure of tethered oligonucleotides containing an internal 3'-phosphoglycolate, 5'-phosphate gapped lesion.

J. Stubbe, C. Turner, H. Junker, 2002, Nucleic acids research.

Why multiple small subunits (Y2 and Y4) for yeast ribonucleotide reductase? Toward understanding the role of Y4

R. Griffin, J. Stubbe, H. Nguyen, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Identification of two alpha-ketoglutarate-dependent dioxygenases in extracts of Rhodotorula glutinis catalyzing deoxyuridine hydroxylation.

J. Stubbe, 1985, The Journal of biological chemistry.

Studies on the catalysis of carbon-cobalt bond homolysis by ribonucleoside triphosphate reductase: evidence for concerted carbon-cobalt bond homolysis and thiyl radical formation.

J. Stubbe, S. Licht, S. Booker, 1999, Biochemistry.

Thermodynamic and kinetic studies on carbon-cobalt bond homolysis by ribonucleoside triphosphate reductase: the importance of entropy in catalysis.

J. Stubbe, S. Licht, C. C. Lawrence, 1999, Biochemistry.

Radicals in biological catalysis.

J. Stubbe, J. Stubbe, 1988, Biochemistry.

Mechanism of Assembly of the Diferric Cluster−Tyrosyl Radical Cofactor of Escherichia coli Ribonucleotide Reductase from the Diferrous Form of the R2 Subunit

J. Stubbe, D. Edmondson, W. Tong, 1996 .

Detection of a new substrate-derived radical during inactivation of ribonucleotide reductase from Escherichia coli by gemcitabine 5'-diphosphate.

J. Stubbe, L. Perez, W. Donk, 1998, Biochemistry.

Mechanism of Assembly of the Tyrosyl Radical-Diiron(III) Cofactorof E. coli Ribonucleotide Reductase. 3. Kinetics of the Limiting Fe2+ Reaction by Optical, EPR, and Moessbauer Spectroscopies

J. Bollinger, J. Stubbe, D. Edmondson, 1994 .

Structure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex

J. Stubbe, Alexander T Taguchi, C. Drennan, 2020, Science.

Glutamate 350 Plays an Essential Role in Conformational Gating of Long-Range Radical Transport in Escherichia coli Class Ia Ribonucleotide Reductase.

K. Yokoyama, D. Nocera, J. Stubbe, 2017, Biochemistry.

Composition and Structure of the Inorganic Core of Relaxed Intermediate X(Y122F) of Escherichia coli Ribonucleotide Reductase.

J. Stubbe, B. Hoffman, M. Shanmugam, 2015, Journal of the American Chemical Society.

Mechanism of assembly of the dimanganese-tyrosyl radical cofactor of class Ib ribonucleotide reductase: enzymatic generation of superoxide is required for tyrosine oxidation via a Mn(III)Mn(IV) intermediate.

J. Stubbe, R. D. Britt, J. Cotruvo, 2013, Journal of the American Chemical Society.

Use of 2,3,5-F(3)Y-β2 and 3-NH(2)Y-α2 to study proton-coupled electron transfer in Escherichia coli ribonucleotide reductase.

J. Stubbe, M. Seyedsayamdost, C. S. Yee, 2011, Biochemistry.

Class I ribonucleotide reductases: metallocofactor assembly and repair in vitro and in vivo.

J. Stubbe, J. Cotruvo, 2011, Annual review of biochemistry.

Identification of protonated oxygenic ligands of ribonucleotide reductase intermediate X.

J. Stubbe, B. Hoffman, M. Shanmugam, 2009, Journal of the American Chemical Society.

pH Dependence of charge transfer between tryptophan and tyrosine in dipeptides.

D. Nocera, Steven Y. Reece, J. Stubbe, 2005, Biochimica et biophysica acta.

Di-iron-tyrosyl radical ribonucleotide reductases.

J. Stubbe, 2003, Current opinion in chemical biology.

Purification of ribonucleotide reductase subunits Y1, Y2, Y3, and Y4 from yeast: Y4 plays a key role in diiron cluster assembly.

J. Stubbe, H. Nguyen, D. Perlstein, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Use of rapid kinetics methods to study the assembly of the diferric-tyrosyl radical cofactor of E. coli ribonucleotide reductase.

J. Bollinger, J. Stubbe, D. Edmondson, 1995, Methods in enzymology.

Class I and III polyhydroxyalkanoate synthases from Ralstonia eutropha and Allochromatium vinosum: characterization and substrate specificity studies.

C. Walsh, A. Sinskey, J. Stubbe, 2001, Archives of biochemistry and biophysics.

Inactivation of Lactobacillus leichmannii ribonucleotide reductase by F2CTP: covalent modification

J. Stubbe, G. Lohman, 2010 .

Inactivation of Lactobacillus leichmannii ribonucleotide reductase by 2',2'-difluoro-2'-deoxycytidine 5'-triphosphate: covalent modification.

J. Stubbe, G. Lohman, 2010, Biochemistry.

2'-Deoxy-2'-methylenecytidine and 2'-deoxy-2',2'-difluorocytidine 5'-diphosphates: potent mechanism-based inhibitors of ribonucleotide reductase.

J. Bollinger, J. Stubbe, C. H. Baker, 1991, Journal of medicinal chemistry.

Polyhydroxybutyrate Synthase: Evidence for Covalent Catalysis

K. Biemann, A. Sinskey, J. Stubbe, 1996 .

The mechanism of free base formation from DNA by bleomycin. A proposal based on site specific tritium release from Poly(dA.dU).

J. Stubbe, J. Kozarich, J. Wu, 1983, The Journal of biological chemistry.

Nontemplate-dependent polymerization processes: polyhydroxyalkanoate synthases as a paradigm.

A. Sinskey, J. Stubbe, Pinghua Liu, 2005, Annual review of biochemistry.

Mono-, di-, tri-, and tetra-substituted fluorotyrosines: new probes for enzymes that use tyrosyl radicals in catalysis.

D. Nocera, Steven Y. Reece, J. Stubbe, 2006, Journal of the American Chemical Society.

X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli.

J. Stubbe, S. Ealick, T. J. Kappock, 1998, Biochemistry.

Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography.

R. Anand, J. Stubbe, S. Ealick, 2004, Biochemistry.

Non-Kramers ESEEM of integer-spin diferrous carboxylate-bridged clusters in proteins

S. Lippard, J. Stubbe, B. Hoffman, 1997 .

Structures of the yeast ribonucleotide reductase Rnr2 and Rnr4 homodimers.

A. Rosenzweig, J. Stubbe, D. Perlstein, 2004, Biochemistry.

Ribonucleotide Reductases: Structure, Chemistry, and Metabolism Suggest New Therapeutic Targets.

D. Nocera, J. Stubbe, M. Bennati, 2020, Annual review of biochemistry.

The core structure of X generated in the assembly of the diiron cluster of ribonucleotide reductase: 17O2 and H217O ENDOR

J. Stubbe, B. Hoffman, W. Antholine, 1998 .

The Ralstonia eutropha PhaR Protein Couples Synthesis of the PhaP Phasin to the Presence of Polyhydroxybutyrate in Cells and Promotes Polyhydroxybutyrate Production

A. Sinskey, J. Stubbe, G. York, 2002, Journal of bacteriology.

Synthesis of Polyhydroxybutyrate in Promoting Ralstonia eutropha Phasin of New Insight into the Role of the PhaP

A. Sinskey, J. Stubbe, G. York, 2001 .

New Insight into the Role of the PhaP Phasin of Ralstonia eutropha in Promoting Synthesis of Polyhydroxybutyrate

A. Sinskey, J. Stubbe, G. York, 2001, Journal of bacteriology.

Determination of the in vivo stoichiometry of tyrosyl radical per ββ' in Saccharomyces cerevisiae ribonucleotide reductase

J. Stubbe, D. Perlstein, Deborah L. Perlstein, 2006 .

Accurate and rapid modeling of iron-bleomycin-induced DNA damage using tethered duplex oligonucleotides and electrospray ionization ion trap mass spectrometric analysis.

J. Stubbe, P. Vouros, A. Harsch, 2000, Nucleic acids research.

Synthesis and characterization of oligonucleotides containing a 4'-keto abasic site.

J. Stubbe, Jingyang Chen, 2004, Biochemistry.

Chemistry with an Artificial Primer of Polyhydroxybutyrate Synthase Suggests a Mechanism for Chain Termination

J. Stubbe, R. Buckley, 2015, Biochemistry.

3.3-Å resolution cryo-EM structure of human ribonucleotide reductase with substrate and allosteric regulators bound

P. Penczek, F. Asturias, K. Tsai, 2018, eLife.

The function of adenosylcobalamin in the mechanism of ribonucleoside triphosphate reductase from Lactobacillus leichmannii.

J. Stubbe, C. C. Lawrence, JoAnne Stubbe, 1998, Current opinion in chemical biology.

Clofarabine targets the large subunit (α) of human ribonucleotide reductase in live cells by assembly into persistent hexamers.

F. Asturias, E. Brignole, J. Stubbe, 2012, Chemistry & biology.

Photochemical Generation of a Tryptophan Radical within the Subunit Interface of Ribonucleotide Reductase.

D. Nocera, J. Stubbe, Brandon L. Greene, 2016, Biochemistry.

Reversible, long-range radical transfer in E. coli class Ia ribonucleotide reductase.

D. Nocera, J. Stubbe, E. Minnihan, 2013, Accounts of chemical research.

Use of 3-aminotyrosine to examine the pathway dependence of radical propagation in Escherichia coli ribonucleotide reductase.

J. Stubbe, M. Seyedsayamdost, E. Minnihan, 2009, Biochemistry.

Incorporation of fluorotyrosines into ribonucleotide reductase using an evolved, polyspecific aminoacyl-tRNA synthetase.

P. Schultz, J. Stubbe, D. Young, 2011, Journal of the American Chemical Society.

Mechanism of action of enolase: effect of the beta-hydroxy group on the rate of dissociation of the alpha-carbon-hydrogen bond.

J. Stubbe, R. Abeles, 1980, Biochemistry.

Cloning, sequencing, and expression of the adenosylcobalamin-dependent ribonucleotide reductase from Lactobacillus leichmannii.

J. Stubbe, S. Booker, 1993, Proceedings of the National Academy of Sciences of the United States of America.

Substrate specificity of formylglycinamidine synthetase.

J. Stubbe, F. Schendel, 1986, Biochemistry.

Enhanced subunit interactions with gemcitabine-5′-diphosphate inhibit ribonucleotide reductases

J. Stubbe, G. Lohman, Jun Wang, 2007, Proceedings of the National Academy of Sciences.

The diferric-tyrosyl radical cluster of ribonucleotide reductase and cytosolic iron-sulfur clusters have distinct and similar biogenesis requirements

J. Stubbe, R. Lill, Caiguo Zhang, 2017, The Journal of Biological Chemistry.

Mechanistic Studies of Semicarbazone Triapine Targeting Human Ribonucleotide Reductase in Vitro and in Mammalian Cells

J. Stubbe, M. Long, Y. Aye, 2012, The Journal of Biological Chemistry.

Bleomycins: towards better therapeutics

J. Stubbe, Jingyang Chen, 2005, Nature Reviews Cancer.

BLEOMYCINS : A STRUCTURAL MODEL FOR SPECIFICITY, BINDING, AND DOUBLE STRAND CLEAVAGE

D. Vanderwall, Wei Wu, J. Stubbe, 1996 .

Investigation of the ATP binding site of Escherichia coli aminoimidazole ribonucleotide synthetase using affinity labeling and site-directed mutagenesis.

J. Stubbe, S. Ealick, S. Oh, 1999, Biochemistry.

Neocarzinostatin-induced hydrogen atom abstraction from C-4' and C-5' of the T residue at a d(GT) step in oligonucleotides: shuttling between deoxyribose attack sites based on isotope selection effects.

J. Stubbe, J. Kozarich, I. Goldberg, 1991, Biochemistry.

Mechanism of bleomycin: evidence for 4'-ketone formation in poly(dA-dU) associated exclusively with free base release.

J. Stubbe, J. Kozarich, J. Wu, 1985, Biochemistry.

19F Electron-Nuclear Double Resonance Reveals Interaction between Redox-Active Tyrosines across the α/β Interface of E. coli Ribonucleotide Reductase

K. Pan, H. Urlaub, J. Stubbe, 2022, Journal of the American Chemical Society.

One of Nature's Macromolecular Machines Demystified

J. Stubbe, 1996, Science.

Genetic Characterization and Role in Virulence of the Ribonucleotide Reductases of Streptococcus sanguinis * ♦

O. Makhlynets, J. Stubbe, P. Xu, 2013, The Journal of Biological Chemistry.

Choosing the Right Metal: Case Studies of Class I Ribonucleotide Reductases*

J. Stubbe, M. J. Parker, Mingxia Huang, 2014, The Journal of Biological Chemistry.

Isotope effects on the cleavage of DNA by bleomycin: mechanism and modulation.

M. Absalon, J. Stubbe, J. Kozarich, 1993, Biochemistry.

Isotope effects of the sequence-specific cleavage of DNA by neocarzinostatin : kinetic partitioning between 4'- and 5'-hydrogen abstraction at unique thymidine sites

J. Stubbe, J. Kozarich, I. Goldberg, 1991 .

Isotope effects on the sequence-specific cleavage of dC in d(AGC) sequences by neocarzinostatin: elucidation of chemistry of minor lesions

J. Stubbe, J. Kozarich, S. H. Wu, 1990 .

An active dimanganese(III)-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase.

J. Stubbe, J. Cotruvo, 2010, Biochemistry.

Mechanism-based inhibition of a mutant Escherichia coli ribonucleotide reductase (cysteine-225----serine) by its substrate CDP.

J. Bollinger, J. Stubbe, S. Mao, 1989, Proceedings of the National Academy of Sciences of the United States of America.

Characterization and chemical properties of phosphoribosylamine, an unstable intermediate in the de novo purine biosynthetic pathway.

S. Wehrli, J. Stubbe, J. Otvos, 1988, Biochemistry.

Biophysical Characterization of Fluorotyrosine Probes Site-Specifically Incorporated into Enzymes: E. coli Ribonucleotide Reductase As an Example

J. Stubbe, R. D. Britt, C. Drennan, 2016, Journal of the American Chemical Society.

Insight into the Mechanism of Inactivation of Ribonucleotide Reductase by Gemcitabine 5#-Diphosphate in the Presence or Absence of Reductant into

J. Stubbe, G. Lohman, K. Yokoyama, 2010 .

Insight into the mechanism of inactivation of ribonucleotide reductase by gemcitabine 5'-diphosphate in the presence or absence of reductant.

R. Griffin, K. Yokoyama, J. Stubbe, 2009, Biochemistry.

Methodology to probe subunit interactions in ribonucleotide reductases.

J. Stubbe, A. Q. Hassan, Yongting Wang, 2008, Biochemistry.

Structural Basis for Activation of Class Ib Ribonucleotide Reductase

A. Rosenzweig, J. Stubbe, J. Cotruvo, 2010, Science.

EXAFS Characterization of the Intermediate X Generated During the Assembly of the Escherichia coli Ribonucleotide Reductase R2 Diferric Tyrosyl Radical Cofactor

L. Que, J. Stubbe, B. Huynh, 1998 .

Unmasking the chemistry of DNA cleavage by the esperamicins : modulation of 4'-hydrogen abstraction and bistranded damage by the fucose-anthranilate moiety

J. Stubbe, I. E. Rosenberg, J. Kozarich, 1992 .

An ENDOR study of the tyrosyl free radical in ribonucleotide reductase from Escherichia coli

T. K. Chandrashekar, M. Sahlin, J. Stubbe, 1989 .

Polyhydroxyalkanoate (PHA) homeostasis: the role of the PHA synthase

J. Stubbe, Jiamin Tian, 2003 .

Clofarabine 5′-di and -triphosphates inhibit human ribonucleotide reductase by altering the quaternary structure of its large subunit

J. Stubbe, Y. Aye, 2011, Proceedings of the National Academy of Sciences.

Mechanism of inactivation of human ribonucleotide reductase with p53R2 by gemcitabine 5'-diphosphate.

J. Stubbe, G. Lohman, Jun Wang, 2009, Biochemistry.

Purification of polyhydroxybutyrate synthase from its native organism, Ralstonia eutropha: implications for the initiation and elongation of polymer formation in vivo.

A. Sinskey, J. Stubbe, C. Brigham, 2012, Biochemistry.

In vitro analysis of the chain termination reaction in the synthesis of poly-(R)-beta-hydroxybutyrate by the class III synthase from Allochromatium vinosum.

A. Sinskey, C. Rha, J. Stubbe, 2005, Biomacromolecules.

PHA synthase activity controls the molecular weight and polydispersity of polyhydroxybutyrate in vivo

A. Sinskey, C. Rha, S. Sim, 1997, Nature Biotechnology.

Overexpression and purification of the soluble polyhydroxyalkanoate synthase from Alcaligenes eutrophus: evidence for a required posttranslational modification for catalytic activity.

A. Sinskey, J. Stubbe, T. Gerngross, 1994, Biochemistry.

The active form of the Saccharomyces cerevisiae ribonucleotide reductase small subunit is a heterodimer in vitro and in vivo.

J. Stubbe, D. Perlstein, Deborah L. Perlstein, 2005, Biochemistry.

Bleomycins: new methods will allow reinvestigation of old issues.

J. Stubbe, Jingyang Chen, 2004, Current opinion in chemical biology.

Mechanistic Insight with HBCH2CoA as a Probe to Polyhydroxybutyrate (PHB) Synthases

J. Stubbe, S. Bossmann, Wei Zhang, 2014, ACS chemical biology.

Mechanistic Insight with HBCH[subscript 2]CoA as a Probe to Polyhydroxybutyrate (PHB) Synthases

J. Stubbe, S. Bossmann, Wei Zhang, 2014 .

Detection of covalent and noncovalent intermediates in the polymerization reaction catalyzed by a C149S class III polyhydroxybutyrate synthase.

J. Stubbe, S. Chakraborty, Ping Li, 2009, Biochemistry.

Investigation of in Vivo Roles of the C-terminal Tails of the Small Subunit (ββ′) of Saccharomyces cerevisiae Ribonucleotide Reductase

J. Stubbe, Xiuxiang An, Mingxia Huang, 2013, The Journal of Biological Chemistry.

Investigation of in Vivo Diferric Tyrosyl Radical Formation in Saccharomyces cerevisiae Rnr2 Protein

J. Stubbe, Lili Liu, Xiaorong Wu, 2011, The Journal of Biological Chemistry.

N5-carboxyaminoimidazole ribonucleotide: evidence for a new intermediate and two new enzymatic activities in the de novo purine biosynthetic pathway of Escherichia coli.

J. Rudolph, V. Davisson, J. Stubbe, 1994, Biochemistry.

Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase

F. Asturias, K. Yokoyama, E. Brignole, 2011, Proceedings of the National Academy of Sciences.

Mechanism of bleomycin: evidence for a rate-determining 4'-hydrogen abstraction from poly(dA-dU) associated with the formation of both free base and base propenal.

J. Stubbe, J. Kozarich, J. Wu, 1985, Biochemistry.

Purification and characterization of aminoimidazole ribonucleotide synthetase from Escherichia coli.

J. Stubbe, J. Smith, F. Schendel, 1986, Biochemistry.

Protein Radicals in Enzyme Catalysis. [Chem. Rev. 1998, 98, 705minus sign762.

J. Stubbe, W. A. van der Donk, 1998, Chemical reviews.

Evidence for the direct transfer of the carboxylate of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to generate 4-carboxy-5-aminoimidazole ribonucleotide catalyzed by Escherichia coli PurE, an N5-CAIR mutase.

J. Stubbe, E. Meyer, T. J. Kappock, 1999, Biochemistry.

Effects of hypoxanthine substitution on bleomycin-mediated DNA strand degradation in DNA-RNA hybrids.

M. Bansal, J. Stubbe, J. Kozarich, 1997, Nucleic acids research.

Mechanistic analyses of site-specific degradation in DNA-RNA hybrids by prototypic DNA cleavers.

M. Bansal, J. Stubbe, J. Kozarich, 1997, Nucleic acids research.

Stereochemical studies of the beta-elimination reactions at aldehydic abasic sites in DNA: endonuclease III from Escherichia coli, sodium hydroxide, and Lys-Trp-Lys.

J. Gerlt, M. Absalon, R. Cunningham, 1991, Biochemistry.

Radicals in Biology: Your Life Is in Their Hands.

D. Nocera, J. Stubbe, 2021, Journal of the American Chemical Society.

Gated Proton Release during Radical Transfer at the Subunit Interface of Ribonucleotide Reductase.

D. Nocera, J. Stubbe, C. Drennan, 2020, Journal of the American Chemical Society.

Isolation of a multifunctional protein with aminoimidazole ribonucleotide synthetase, glycinamide ribonucleotide synthetase, and glycinamide ribonucleotide transformylase activities: characterization of aminoimidazole ribonucleotide synthetase.

J. Stubbe, F. Schendel, J. Schrimsher, 1986, Biochemistry.

Polyhydroxyalkanoate (PHA) hemeostasis: the role of PHA synthase.

J. Stubbe, Jiamin Tian, 2003, Natural product reports.

Immunocytochemical analysis of poly-beta-hydroxybutyrate (PHB) synthase in Alcaligenes eutrophus H16: localization of the synthase enzyme at the surface of PHB granules

A. Sinskey, J. Stubbe, T. Gerngross, 1993, Journal of bacteriology.

Class III polyhydroxybutyrate synthase: involvement in chain termination and reinitiation.

A. Sinskey, J. Stubbe, Jiamin Tian, 2005, Biochemistry.

Detection of intermediates from the polymerization reaction catalyzed by a D302A mutant of class III polyhydroxyalkanoate (PHA) synthase.

A. Sinskey, J. Stubbe, Jiamin Tian, 2005, Biochemistry.

Mechanistic studies on class I polyhydroxybutyrate (PHB) synthase from Ralstonia eutropha: class I and III synthases share a similar catalytic mechanism.

A. Sinskey, J. Stubbe, W. Yuan, 2001, Biochemistry.

The formylglycinamide ribonucleotide amidotransferase complex from Bacillus subtilis: metabolite-mediated complex formation.

R. Anand, J. Stubbe, S. Ealick, 2004, Biochemistry.

A multifunctional protein possessing glycinamide ribonucleotide synthetase, glycinamide ribonucleotide transformylase, and aminoimidazole ribonucleotide synthetase activities in de novo purine biosynthesis.

S. Henikoff, S. Benkovic, J. Stubbe, 1985, Biochemistry.

Site-specific insertion of 3-aminotyrosine into subunit alpha2 of E. coli ribonucleotide reductase: direct evidence for involvement of Y730 and Y731 in radical propagation.

Clement T Y Chan, P. Schultz, J. Xie, 2007, Journal of the American Chemical Society.

Solution structure of the hydroperoxide of Co(III) phleomycin complexed with d(CCAGGCCTGG)2: evidence for binding by partial intercalation.

D. Vanderwall, Wei Wu, J. Stubbe, 2002, Nucleic acids research.

NONTEMPLATE-DEPENDENT POLYMERIZATION

A. Sinskey, J. Stubbe, Pinghua Liu, 2005 .

GC/MS methods to quantify the 2-deoxypentos-4-ulose and 3'-phosphoglycolate pathways of 4' oxidation of 2-deoxyribose in DNA: application to DNA damage produced by gamma radiation and bleomycin.

J. Stubbe, P. Dedon, Xinfeng Zhou, 2007, Chemical research in toxicology.

STRUCTURAL CHARACTERIZATION OF CO.BLEOMYCIN A2 BROWN : FREE AND BOUND TO D(CCAGGCCTGG)

D. Vanderwall, Wei Wu, J. Stubbe, 1997 .

Studies of Co·Bleomycin A2 Green: Its Detailed Structural Characterization by NMR and Molecular Modeling and Its Sequence-Specific Interaction with DNA Oligonucleotides

D. Vanderwall, Wei Wu, J. Stubbe, 1996 .

Exafs studies of binuclear iron proteins hemerythrin and ribonucleotide reductase

L. Que, J. Stubbe, A. Roe, 1987 .

Reconsideration of X, the Diiron Intermediate Formed during Cofactor Assembly in E. coli Ribonucleotide Reductase

JoAnne Stubbe, J. Stubbe, B. Hoffman, 1996 .

Dinuclear non-heme iron centers: structure and function

J. Stubbe, 1991 .

Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase.

J. Bollinger, J. Stubbe, D. Edmondson, 1991, Science.

Mechanisms of bleomycin-induced DNA degradation

J. Stubbe, J. Kozarich, 1987 .

Ribonucleotide reductases: amazing and confusing.

J. Stubbe, J Stubbe, 1990, The Journal of biological chemistry.

Structural Examination of the Transient 3-Aminotyrosyl Radical on the PCET Pathway of E. coli Ribonucleotide Reductase by Multifrequency EPR Spectroscopy

J. Stubbe, M. Bennati, M. Seyedsayamdost, 2009, Journal of the American Chemical Society.

Protein Radicals in Enzyme Catalysis.

J. Stubbe, W. A. van der Donk, 1998, Chemical reviews.

Radical initiation in the class I ribonucleotide reductase: long-range proton-coupled electron transfer?

Michelle C. Y. Chang, D. Nocera, J. Stubbe, 2003, Chemical reviews.

5.08 – Mechanistic Investigations of Ribonucleotide Reductases

J. Stubbe, S. Licht, 1999 .

Mechanism-based inactivation of thymine hydroxylase, an alpha-ketoglutarate-dependent dioxygenase, by 5-ethynyluracil.

J. Stubbe, L. D. Thornburg, 1993, Biochemistry.

Thiyl Radicals in Ribonucleotide Reductases

J. Stubbe, S. Licht, G. Gerfen, 1996, Science.

Characterization of C439SR1, a mutant of Escherichia coli ribonucleotide diphosphate reductase: evidence that C439 is a residue essential for nucleotide reduction and C439SR1 is a protein possessing novel thioredoxin-like activity.

J. Stubbe, S. Mao, G. Yu, 1992, Biochemistry.

Location of the redox-active thiols of ribonucleotide reductase: sequence similarity between the Escherichia coli and Lactobacillus leichmannii enzymes.

J. Stubbe, G. Ashley, A. Lin, 1987, Biochemistry.

Conserved electron donor complex Dre2–Tah18 is required for ribonucleotide reductase metallocofactor assembly and DNA synthesis

J. Stubbe, Lili Liu, Caiguo Zhang, 2014, Proceedings of the National Academy of Sciences.

Metallation and mismetallation of iron and manganese proteins in vitro and in vivo: the class I ribonucleotide reductases as a case study.

J. Stubbe, J. Cotruvo, 2012, Metallomics : integrated biometal science.

The dimanganese(II) site of Bacillus subtilis class Ib ribonucleotide reductase.

A. Rosenzweig, J. Stubbe, J. Cotruvo, 2012, Biochemistry.

Control of metallation and active cofactor assembly in the class Ia and Ib ribonucleotide reductases: diiron or dimanganese?

J. Stubbe, J. Cotruvo, 2011, Current opinion in chemical biology.

Escherichia coli class Ib ribonucleotide reductase contains a dimanganese(III)-tyrosyl radical cofactor in vivo.

J. Stubbe, J. Cotruvo, 2011, Biochemistry.

Binuclear Manganese(III) Complexes of Potential Biological Significance

S. Lippard, J. Stubbe, G. Dismukes, 1987 .

Radicals with a controlled lifestyle.

J. Stubbe, 2003, Chemical communications.

Solution Structure of Co·Bleomycin A2 Green Complexed with d(CCAGGCCTGG)

D. Vanderwall, Wei Wu, J. Stubbe, 1996 .

Interaction of Co.cntdot.Bleomycin A2 (Green) with d(CCAGGCCTGG)2: Evidence for Intercalation Using 2D NMR

D. Vanderwall, Wei Wu, J. Stubbe, 1994 .

Protein radical involvement in biological catalysis?

J. Stubbe, 1989, Annual review of biochemistry.

Direct observation of a transient tyrosine radical competent for initiating turnover in a photochemical ribonucleotide reductase.

D. Nocera, Steven Y. Reece, J. Stubbe, 2007, Journal of the American Chemical Society.

Site-specific incorporation of fluorotyrosines into the R2 subunit of E. coli ribonucleotide reductase by expressed protein ligation

J. Stubbe, M. Seyedsayamdost, C. S. Yee, 2007, Nature Protocols.

Analogs of phosphoenolpyruvate. On the specificity of pyruvate kinase from rabbit muscle.

G. L. Kenyon, J. Stubbe, 1971, Biochemistry.

A non-heme iron protein with heme tendencies: an investigation of the substrate specificity of thymine hydroxylase.

M. Lai, J. Stubbe, J. Wishnok, 1993, Biochemistry.

Novel diferric radical intermediate responsible for tyrosyl radical formation in assembly of the cofactor of ribonucleotide reductase

J. Bollinger, J. Stubbe, D. Edmondson, 1991 .

DNA degradation by bleomycin: evidence for 2'R-proton abstraction and for C-O bond cleavage accompanying base propenal formation.

J. Stubbe, J. Kozarich, J. Wu, 1986, Biochemistry.

Identification of the alkaline-labile product accompanying cytosine release during bleomycin-mediated degradation of d(CGCGCG)

J. Gerlt, J. Stubbe, J. Kozarich, 1986 .

Harnessing free radicals: formation and function of the tyrosyl radical in ribonucleotide reductase.

J. Stubbe, P. Riggs-Gelasco, 1998, Trends in biochemical sciences.

Selenocysteine Substitution into a Class I Ribonucleotide Reductase.

D. Nocera, J. Stubbe, Brandon L. Greene, 2019, Biochemistry.

X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution.

J. Stubbe, S. Ealick, T. J. Kappock, 1999, Structure.

Proton-coupled electron transfer: the mechanistic underpinning for radical transport and catalysis in biology

D. Nocera, Steven Y. Reece, J. Hodgkiss, 2006, Philosophical Transactions of the Royal Society B: Biological Sciences.

Chemical characterization of phosphoribosylamine, a substrate for newly discovered trifunctional protein containing glycineamide ribonucleotide synthetase activity.

S. Wehrli, J. Stubbe, J. Otvos, 1987, Advances in enzyme regulation.

Current ideas on the chemical mechanism of ribonucleotide reductases.

J. Stubbe, G. Ashley, 1985, Pharmacology & therapeutics.

Inactivation of Lactobacillus leichmannii ribonucleotide reductase by F2CTP: adenosylcobalamin destruction and formation of a nucleotide based radical

J. Stubbe, G. Gerfen, G. Lohman, 2010 .

High-frequency (140-GHz) time domain EPR and ENDOR spectroscopy: the tyrosyl radical-diiron cofactor in ribonucleotide reductase from yeast.

R. Griffin, J. Stubbe, M. Bennati, 2001, Journal of the American Chemical Society.

Adenosylcobalamin-Dependent Ribonucleotide Reductases: Still Amazing but No Longer Confusing

J. Stubbe, S. Licht, G. Gerfen, 2007 .

High-frequency EPR and ENDOR: Time-domain spectroscopy of ribonucleotide reductase

R. Griffin, J. Stubbe, M. Bennati, 2001 .

High-field EPR detection of a disulfide radical anion in the reduction of cytidine 5'-diphosphate by the E441Q R1 mutant of Escherichia coli ribonucleotide reductase.

R. Griffin, J. Stubbe, M. Bennati, 1999, Proceedings of the National Academy of Sciences of the United States of America.

Structure of the Nucleotide Radical Formed during Reaction of CDP/TTP with the E441Q-α2β2 of E. coli Ribonucleotide Reductase

R. Griffin, J. Stubbe, S. Kacprzak, 2008, Journal of the American Chemical Society.

The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer

M. Sintchak, J. Stubbe, C. Drennan, 2002, Nature Structural Biology.

Class II Ribonucleotide Reductases Catalyze Carbon−Cobalt Bond Reformation on Every Turnover

J. Stubbe, S. Licht, C. C. Lawrence, 1999 .

Characterization of a substrate-derived radical detected during the inactivation of ribonucleotide reductase from Escherichia coli by 2'- fluoromethylene-2'-deoxycytidine 5'-diphosphate

R. Griffin, J. Stubbe, C. Farrar, 1998 .

Gemcitabine 5'-triphosphate is a stoichiometric mechanism-based inhibitor of Lactobacillus leichmannii ribonucleoside triphosphate reductase: evidence for thiyl radical-mediated nucleotide radical formation.

J. Stubbe, D. J. Silva, V. Samano, 1998, Biochemistry.

EPR Investigations of the Inactivation of E. coli Ribonucleotide Reductase with 2'-Azido-2'-deoxyuridine 5'-Diphosphate: Evidence for the Involvement of the Thiyl Radical of C225-R1

Robert G. Griffin, JoAnne Stubbe, R. Griffin, 1995 .

Coenzyme B12-dependent ribonucleotide reductase: evidence for the participation of five cysteine residues in ribonucleotide reduction.

J. Stubbe, S. Licht, S. Booker, 1994, Biochemistry.

Ribonucleotide reductases: radical enzymes with suicidal tendencies.

J. Stubbe, S. Booker, J. Broderick, 1995, Biochemical Society transactions.

2'-Deoxy-2'-halonucleotides as alternate substrates and mechanism-based inactivators of Lactobacillus leichmannii ribonucleotide reductase.

J. Stubbe, G. Ashley, R. Tolman, 1987, Biochemistry.

Mechanism of inactivation of Escherichia coli ribonucleotide reductase by 2'-chloro-2'-deoxyuridine 5'-diphosphate: evidence for generation of a 2'-deoxy-3'-ketonucleotide via a net 1,2 hydrogen shift.

J. Stubbe, M. Ator, 1985, Biochemistry.

Mechanism of inactivation of Escherichia coli and Lactobacillus leichmannii ribonucleotide reductases by 2'-chloro-2'-deoxynucleotides: evidence for generation of 2-methylene-3(2H)-furanone.

J. Stubbe, J Stubbe, G Harris, 1984, Biochemistry.

Equilibration of tyrosyl radicals (Y356•, Y731•, Y730•) in the radical propagation pathway of the Escherichia coli class Ia ribonucleotide reductase.

R. Griffin, K. Yokoyama, J. Stubbe, 2011, Journal of the American Chemical Society.

High-field pulsed electron–electron double resonance spectroscopy to determine the orientation of the tyrosyl radicals in ribonucleotide reductase

V. Denysenkov, J. Stubbe, M. Bennati, 2006, Proceedings of the National Academy of Sciences.

Are carboxylations involving biotin concerted or nonconcerted?

J. Stubbe, R. Abeles, S. Fish, 1980, The Journal of biological chemistry.

Bacillus subtilis class Ib ribonucleotide reductase is a dimanganese(III)-tyrosyl radical enzyme.

J. Stubbe, Yan Zhang, 2011, Biochemistry.

Redox-linked structural changes in ribonucleotide reductase.

J. Stubbe, A. Offenbacher, M. Seyedsayamdost, 2009, Journal of the American Chemical Society.

NrdI, a flavodoxin involved in maintenance of the diferric-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase

Joseph A Cotruvo, JoAnne Stubbe, J. Stubbe, 2008, Proceedings of the National Academy of Sciences.

High-frequency (139.5 GHz) EPR spectroscopy of the tyrosyl radical in Escherichia coli ribonucleotide reductase

D. Singel, R. Griffin, J. Bollinger, 1993 .

Binding of Cob(II)alamin to the adenosylcobalamin-dependent ribonucleotide reductase from Lactobacillus leichmannii. Identification of dimethylbenzimidazole as the axial ligand.

J. Stubbe, G. Gerfen, V. Samano, 1999, The Journal of biological chemistry.

Accumulation of the PhaP Phasin of Ralstonia eutropha Is Dependent on Production of Polyhydroxybutyrate in Cells

Björn H. Junker, A. Sinskey, J. Stubbe, 2001, Journal of bacteriology.

Direct interfacial Y731 oxidation in α2 by a photoβ2 subunit of E. coli class Ia ribonucleotide reductase

D. Nocera, J. Stubbe, Patrick G. Holder, 2015, Chemical science.

Kinetics of Hydrogen Atom Abstraction from Substrate by an Active Site Thiyl Radical in Ribonucleotide Reductase

D. Nocera, J. Stubbe, Yifeng Wei, 2014, Journal of the American Chemical Society.

A model of the structure of HOO-Co.bleomycin bound to d(CCAGTACTGG): recognition at the d(GpT) site and implications for double-stranded DNA cleavage.

D. Vanderwall, J. Stubbe, J. Kozarich, 1997, Chemistry & biology.

Sequence-specific isotope effects on the cleavage of DNA by bleomycin.

D. Vanderwall, J. Stubbe, J. Kozarich, 1989, Science.

Formal Reduction Potentials of Difluorotyrosine and Trifluorotyrosine Protein Residues: Defining the Thermodynamics of Multistep Radical Transfer.

C. Tommos, D. Nocera, J. Stubbe, 2017, Journal of the American Chemical Society.

Glutamate 350 plays an essential role in conformational gating of long range radical transport in E. coli class Ia ribonucleotide reductase

J. Stubbe, J. Shao, K. Yokoyama, 2017 .

A >200 meV Uphill Thermodynamic Landscape for Radical Transport in Escherichia coli Ribonucleotide Reductase Determined Using Fluorotyrosine-Substituted Enzymes.

C. Tommos, D. Nocera, J. Stubbe, 2016, Journal of the American Chemical Society.

Charge-Transfer Dynamics at the α/β Subunit Interface of a Photochemical Ribonucleotide Reductase.

D. Nocera, J. Stubbe, L. Olshansky, 2016, Journal of the American Chemical Society.

Reverse Electron Transfer Completes the Catalytic Cycle in a 2,3,5-Trifluorotyrosine-Substituted Ribonucleotide Reductase

D. Nocera, J. Stubbe, K. Ravichandran, 2015, Journal of the American Chemical Society.

Formal reduction potential of 3,5-difluorotyrosine in a structured protein: insight into multistep radical transfer.

C. Tommos, J. Stubbe, K. Ravichandran, 2013, Biochemistry.

Photoactive peptides for light-initiated tyrosyl radical generation and transport into ribonucleotide reductase.

D. Nocera, Steven Y. Reece, J. Stubbe, 2007, Journal of the American Chemical Society.

pH Rate profiles of FnY356-R2s (n = 2, 3, 4) in Escherichia coli ribonucleotide reductase: evidence that Y356 is a redox-active amino acid along the radical propagation pathway.

D. Nocera, Steven Y. Reece, J. Stubbe, 2006, Journal of the American Chemical Society.

Subcellular localization of yeast ribonucleotide reductase regulated by the DNA replication and damage checkpoint pathways

Zhen Zhang, JoAnne Stubbe, J. Stubbe, 2003, Proceedings of the National Academy of Sciences of the United States of America.

Hydrogen Bond Network between Amino Acid Radical Intermediates on the Proton-Coupled Electron Transfer Pathway of E. coli α2 Ribonucleotide Reductase

F. Neese, J. Stubbe, M. Bennati, 2014, Journal of the American Chemical Society.

Modulation of Y356 photooxidation in E. coli class Ia ribonucleotide reductase by Y731 across the α2:β2 interface.

D. Nocera, J. Stubbe, Patrick G. Holder, 2013, Journal of the American Chemical Society.

Function of the diiron cluster of Escherichia coli class Ia ribonucleotide reductase in proton-coupled electron transfer.

K. Yokoyama, C. Krebs, J. Bollinger, 2013, Journal of the American Chemical Society.

ENDOR spectroscopy and DFT calculations: evidence for the hydrogen-bond network within α2 in the PCET of E. coli ribonucleotide reductase.

F. Neese, J. Stubbe, M. Bennati, 2012, Journal of the American Chemical Society.

Photo-ribonucleotide reductase β2 by selective cysteine labeling with a radical phototrigger

Daniel G Nocera, JoAnne Stubbe, Thomas S. Teets, 2011, Proceedings of the National Academy of Sciences.

Kinetics of radical intermediate formation and deoxynucleotide production in 3-aminotyrosine-substituted Escherichia coli ribonucleotide reductases.

U. Uhlin, J. Stubbe, M. Seyedsayamdost, 2011, Journal of the American Chemical Society.

A hot oxidant, 3-NO2Y122 radical, unmasks conformational gating in ribonucleotide reductase.

U. Uhlin, K. Yokoyama, J. Stubbe, 2010, Journal of the American Chemical Society.

Site-specific incorporation of 3-nitrotyrosine as a probe of pKa perturbation of redox-active tyrosines in ribonucleotide reductase.

U. Uhlin, K. Yokoyama, J. Stubbe, 2010, Journal of the American Chemical Society.

Replacement of Y730 and Y731 in the alpha2 subunit of Escherichia coli ribonucleotide reductase with 3-aminotyrosine using an evolved suppressor tRNA/tRNA-synthetase pair.

J. Stubbe, M. Seyedsayamdost, 2009, Methods in enzymology.

Site-specific replacement of Y356 with 3,4-dihydroxyphenylalanine in the beta2 subunit of E. coli ribonucleotide reductase.

J. Stubbe, M. Seyedsayamdost, 2006, Journal of the American Chemical Society.

Pre-steady-state and steady-state kinetic analysis of E. coli class I ribonucleotide reductase.

J. Stubbe, M. Ator, J. Ge, 2003, Biochemistry.

2,3-difluorotyrosine at position 356 of ribonucleotide reductase R2: a probe of long-range proton-coupled electron transfer.

D. Nocera, J. Stubbe, J. Ge, 2003, Journal of the American Chemical Society.

Ribonucleotide reductases in the twenty-first century.

J. Stubbe, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Mechanism of Assembly of the Tyrosyl Radical-Diiron(III) Cofactorof E. coli Ribonucleotide Reductase. 3. Kinetics of the Limiting Fe2+ Reaction by Optical, EPR, and Moessbauer Spectroscopies

J. Bollinger, J. Stubbe, D. Edmondson, 1994 .

Cloning, overproduction, and purification of the B2 subunit of ribonucleoside-diphosphate reductase

J. Stubbe, S. Salowe, 1986, Journal of bacteriology.

Effect of substrate on the diiron(III) site in stearoyl acyl carrier protein delta 9-desaturase as disclosed by cryoreduction electron paramagnetic resonance/electron nuclear double resonance spectroscopy.

J. Shanklin, J. Stubbe, B. Hoffman, 2005, Biochemistry.

Ribonucleotide reductases.

J. Stubbe, 1990, Advances in enzymology and related areas of molecular biology.

Products of the inactivation of ribonucleoside diphosphate reductase from Escherichia coli with 2'-azido-2'-deoxyuridine 5'-diphosphate.

J. Stubbe, S P Salowe, M A Ator, 1987, Biochemistry.

Mechanism based inactivation of the adenosylcobalamin-dependent ribonucleotide reductase from L. leichmannii by 2′-ara-2′-azido-2′-deoxy adenosine-5′-triphosphate: Observation of paramagnetic intermediates

M. J. Robins, J. Stubbe, G. Ashley, 1997 .

DNA oligonucleotides with A, T, G or C opposite an abasic site: structure and dynamics

D. Case, J. Stubbe, F. Dupradeau, 2007, Nucleic acids research.

High-frequency 180 GHz PELDOR

V. Denysenkov, J. Stubbe, M. Bennati, 2005 .

The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant

J. Stubbe, C. Drennan, Jiyeon Baek, 2014, Proceedings of the National Academy of Sciences.

Controlling radical reactions

J. Stubbe, 1994, Nature.

Alternative model for mechanism-based inhibition of Escherichia coli ribonucleotide reductase by 2'-azido-2'-deoxyuridine 5'-diphosphate.

J. Bollinger, J. Stubbe, J. Peisach, 1993, Biochemistry.

Mechanism of B12-dependent ribonucleotide reductase

J. Stubbe, 2004, Molecular and Cellular Biochemistry.

Nuclear magnetic resonance structural studies and molecular modeling of duplex DNA containing normal and 4'-oxidized abasic sites.

D. Case, J. Stubbe, F. Dupradeau, 2007, Biochemistry.

Identification and quantitation of the lesion accompanying base release in bleomycin-mediated DNA degradation

J. Stubbe, J. Kozarich, L. Rabow, 1990 .

Mechanistic Studies of Bleomycin-Mediated DNA Cleavage Using Isotope Labeling

G. Mcgall, J. Stubbe, 1988 .

Mechanism of ribonucleotide reductase from herpes simplex virus type 1. Evidence for 3' carbon-hydrogen bond cleavage and inactivation by nucleotide analogs.

J. Stubbe, T. Spector, M. Ator, 1986, The Journal of biological chemistry.

On the mechanism of ribonucleoside diphosphate reductase from Escherichia coli. Evidence for 3'-C--H bond cleavage.

J. Stubbe, J Stubbe, D Ackles, 1983, The Journal of biological chemistry.

Inorganic pyrophosphate is released from 2'-chloro-2'-deoxyuridine 5'-diphosphate by ribonucleoside diphosphate reductase

J. Stubbe, J. Kozarich, 1980 .

A model for the role of multiple cysteine residues involved in ribonucleotide reduction: amazing and still confusing.

J. Bollinger, J. Stubbe, S. Booker, 1992, Biochemistry.

Statistical analysis of ENDOR spectra

S. Huckemann, Y. Pokern, J. Stubbe, 2021, Proceedings of the National Academy of Sciences.

The evolution of ribonucleotide reduction revisited.

J. Stubbe, J. Ge, C. S. Yee, 2001, Trends in biochemical sciences.

Identification of the source of oxygen in the alkaline-labile product accompanying cytosine release during bleomycin-mediated oxidative degradation of d(CGCGCG)

G. Mcgall, J. Stubbe, J. Kozarich, 1990 .

Epimerization at carbon-5' of (5'R)-[5'-2H]adenosylcobalamin by ribonucleoside triphosphate reductase: cysteine 408-independent cleavage of the Co-C5' bond.

P. Frey, J. Stubbe, Dawei Chen, 2003, Biochemistry.

Ribonucleotide reductases: radical enzymes with suicidal tendencies.

J. Stubbe, G. Ashley, M. Ator, 1993, Nucleic acids symposium series.

Ribonucleotide reductases: the link between an RNA and a DNA world?

J. Stubbe, 2000, Current opinion in structural biology.

Binding site revealed of nature's most beautiful cofactor.

J. Stubbe, 1994, Science.

The mechanism of Lactobacillus leichmannii ribonucleotide reductase. Evidence for 3' carbon-hydrogen bond cleavage and a unique role for coenzyme B12.

J. Stubbe, G. Ashley, G. Harris, 1986, The Journal of biological chemistry.

Structure of the nitrogen-centered radical formed during inactivation of E. coli ribonucleotide reductase by 2'-azido-2'-deoxyuridine-5'-diphosphate: trapping of the 3'-ketonucleotide.

R. Griffin, J. Stubbe, S. Kacprzak, 2005, Journal of the American Chemical Society.

Inactivation of ribonucleotide reductase by (E)-2'-fluoromethylene-2'-deoxycytidine 5'-diphosphate: a paradigm for nucleotide mechanism-based inhibitors.

J. Stubbe, W. A. van der Donk, J Stubbe, 1996, Biochemistry.

Fluoride, pyrophosphate, and base release from 2'-deoxy-2'-fluoronucleoside 5'-diphosphates by ribonucleoside-diphosphate reductase.

J. Stubbe, J. Kozarich, 1980, The Journal of biological chemistry.

Inactivation of the ribonucleoside triphosphate reductase from Lactobacillus leichmannii by 2'-chloro-2'-deoxyuridine 5'-triphosphate: a 3'-2' hydrogen transfer during the formation of 3'-keto-2'-deoxyuridine 5'-triphosphate.

J. Stubbe, G. Ashley, G. Harris, 1988, Biochemistry.

Inactivation of the Lactobacillus leichmannii ribonucleoside triphosphate reductase by 2'-chloro-2'-deoxyuridine 5'-triphosphate: stoichiometry of inactivation, site of inactivation, and mechanism of the protein chromophore formation.

J. Stubbe, G. Ashley, G. Harris, 1988, Biochemistry.

Interaction of 3'-[3H]2'-Chloro-2'-deoxyuridine 5'-triphosphate with ribonucleotide reductase from Lactobacillus leichmannii.

J. Stubbe, Raymond L. Blakley, G. Smith, 1983, Journal of Biological Chemistry.

On the mechanism of ribonucleoside triphosphate reductase from Lactobacillus leichmannii. Evidence for 3' C--H bond cleavage.

J. Stubbe, Raymond L. Blakley, R. Segal, 1981, Journal of Biological Chemistry.

Mechanistic studies on bleomycin-mediated DNA damage: multiple binding modes can result in double-stranded DNA cleavage

J. Stubbe, Grace E Kenney, Jingyang Chen, 2008, Nucleic acids research.

Analogs of phosphoenolpyruvate. Substrate specificities of enolase and pyruvate kinase from rabbit muscle.

G. L. Kenyon, J. Stubbe, 1972, Biochemistry.

An endogenous dAMP ligand in Bacillus subtilis class Ib RNR promotes assembly of a noncanonical dimer for regulation by dATP

S. Meisburger, W. Thomas, N. Ando, 2018, Proceedings of the National Academy of Sciences.

A Chemically Competent Thiosulfuranyl Radical on the Escherichia coli Class III Ribonucleotide Reductase

Jiahao Chen, R. Griffin, K. Yokoyama, 2014, Journal of the American Chemical Society.

Detection of Water Molecules on the Radical Transfer Pathway of Ribonucleotide Reductase by 17O Electron–Nuclear Double Resonance Spectroscopy

J. Stubbe, M. Bennati, Fabian Hecker, 2021, Journal of the American Chemical Society.

Glycinamide ribonucleotide synthetase from Escherichia coli: cloning, overproduction, sequencing, isolation, and characterization.

J. Rudolph, J. Stubbe, J. Smith, 1990, Biochemistry.

Turning on ribonucleotide reductase by light-initiated amino acid radical generation.

D. Nocera, J. Stubbe, C. S. Yee, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Phage auxiliary metabolic genes and the redirection of cyanobacterial host carbon metabolism.

Katherine H. Huang, Luke R. Thompson, S. Chisholm, 2011, Proceedings of the National Academy of Sciences of the United States of America.

YfaE, a ferredoxin involved in diferric-tyrosyl radical maintenance in Escherichia coli ribonucleotide reductase.

C. Krebs, J. Stubbe, Wei Jiang, 2007, Biochemistry.

Ribonucleotide Reductase: Recent Advances

J. Stubbe, J. Cotruvo, 2008 .

Importance of the Maintenance Pathway in the Regulation of the Activity of Escherichia coli Ribonucleotide Reductase†

C. Krebs, J. Stubbe, Wei Jiang, 2008, Biochemistry.

Reactions catalyzed by 5-aminoimidazole ribonucleotide carboxylases from Escherichia coli and Gallus gallus: a case for divergent catalytic mechanisms.

S M Firestine, V. Davisson, J. Stubbe, 1994, Biochemistry.

Nuclear localization of the Saccharomyces cerevisiae ribonucleotide reductase small subunit requires a karyopherin and a WD40 repeat protein

N. Kelleher, J. Stubbe, L. Hicks, 2006, Proceedings of the National Academy of Sciences of the United States of America.

Ralstonia eutropha H16 Encodes Two and Possibly Three Intracellular Poly[d-(−)-3-Hydroxybutyrate] Depolymerase Genes

A. Sinskey, J. Stubbe, J. Lupberger, 2003, Journal of bacteriology.

Cytosolic monothiol glutaredoxins function in intracellular iron sensing and trafficking via their bound iron-sulfur cluster.

Marta A. Uzarska, E. Herrero, C. Lillig, 2010, Cell metabolism.

N5-CAIR mutase: role of a CO2 binding site and substrate movement in catalysis.

Aaron A Hoskins, Judith B. Zaugg, Akimitsu Okamoto, 2007, Biochemistry.

Deciphering radical transport in the large subunit of class I ribonucleotide reductase.

D. Nocera, J. Stubbe, B. Anderson, 2011, Journal of the American Chemical Society.

Formylglycinamide ribonucleotide synthetase from Escherichia coli: cloning, sequencing, overproduction, isolation, and characterization.

J. Stubbe, A. Shiau, J. Smith, 1989, Biochemistry.

Solution structure of Co(III)-bleomycin-OOH bound to a phosphoglycolate lesion containing oligonucleotide: implications for bleomycin-induced double-strand DNA cleavage.

J. Stubbe, C. Turner, H. Junker, 2001, Biochemistry.

Bacillus subtilis Class Ib Ribonucleotide Reductase: High Activity and Dynamic Subunit Interactions

J. Stubbe, M. J. Parker, Xuling Zhu, 2014, Biochemistry.

Three-dimensional structure of N5-carboxyaminoimidazole ribonucleotide synthetase: a member of the ATP grasp protein superfamily.

J. Thoden, H. Holden, J. Stubbe, 1999, Biochemistry.

Interaction of C225SR1 mutant subunit of ribonucleotide reductase with R2 and nucleoside diphosphates: tales of a suicidal enzyme.

J. Bollinger, J. Stubbe, T. Holler, 1992, Biochemistry.

Investigation of the mechanism of phosphoribosylamine transfer from glutamine phosphoribosylpyrophosphate amidotransferase to glycinamide ribonucleotide synthetase.

J. Rudolph, J. Stubbe, 1995, Biochemistry.

Formylglycinamide Ribonucleotide Amidotransferase from Thermotoga maritima: Structural Insights into Complex Formation†‡

J. Stubbe, M. Morar, S. Ealick, 2008, Biochemistry.

Modular evolution of the purine biosynthetic pathway.

J. Stubbe, S. Ealick, T. J. Kappock, 2000, Current opinion in chemical biology.

Crystal structure of Escherichia coli PurE, an unusual mutase in the purine biosynthetic pathway.

S E Ealick, I. Mathews, J. Stubbe, 1999, Structure.

Allosteric Inhibition of Human Ribonucleotide Reductase by dATP Entails the Stabilization of a Hexamer

F. Asturias, E. Brignole, N. Ando, 2015, Biochemistry.

Complexed structures of formylglycinamide ribonucleotide amidotransferase from Thermotoga maritima describe a novel ATP binding protein superfamily.

R. Anand, J. Stubbe, M. Morar, 2006, Biochemistry.

A model for the Bacillus subtilis formylglycinamide ribonucleotide amidotransferase multiprotein complex.

M. Sintchak, R. Anand, J. Stubbe, 2004, Biochemistry.

Electron paramagnetic resonance investigations of a kinetically competent intermediate formed in ribonucleotide reduction: Evidence for a thiyl radical-cob(II)alamin interaction

J. Stubbe, B. Hoffman, S. Licht, 1996 .

Solution structure of an oligonucleotide containing an abasic site: evidence for an unusual deoxyribose conformation.

J. Stubbe, C. Turner, S. Hoehn, 2001, Nucleic acids research.

Dif1 is a DNA-damage-regulated facilitator of nuclear import for ribonucleotide reductase.

S. Elledge, J. Stubbe, Jun Wang, 2008, Molecular cell.

Unnatural amino acids: better than the real things?

K. Yokoyama, J. Stubbe, E. Minnihan, 2009, F1000 biology reports.

Ribonucleotide reductase, a novel target for gonorrhea

J. Stubbe, J. Narasimhan, A. Branstrom, 2020, bioRxiv.

Design of a Fluoro-olefin Cytidine Nucleoside as a Bioprecursor of a Mechanism-Based Inhibitor of Ribonucleotide Reductase

A. Bitonti, J. Stubbe, P. Sunkara, 1996 .

Streptococcus sanguinis Class Ib Ribonucleotide Reductase

A. Rosenzweig, O. Makhlynets, J. Stubbe, 2013, The Journal of Biological Chemistry.

A Ferredoxin Disulfide Reductase Delivers Electrons to the Methanosarcina barkeri Class III Ribonucleotide Reductase

S. Elliott, J. Ferry, J. Stubbe, 2015, Biochemistry.

Conformational Motions and Water Networks at the α/β Interface in E. coli Ribonucleotide Reductase.

J. Stubbe, Pengfei Li, C. Drennan, 2020, Journal of the American Chemical Society.

Basis of dATP inhibition of RNRs

D. Nocera, J. Stubbe, Brandon L. Greene, 2018, The Journal of Biological Chemistry.

Spectroscopic Evidence for a H Bond Network at Y356 Located at the Subunit Interface of Active E. coli Ribonucleotide Reductase.

J. Stubbe, M. Bennati, K. Ravichandran, 2017, Biochemistry.

Glutamate 52-β at the α/β subunit interface of Escherichia coli class Ia ribonucleotide reductase is essential for conformational gating of radical transfer

J. Stubbe, C. Drennan, J. Shao, 2017, The Journal of Biological Chemistry.

Radical transfer in E. coli ribonucleotide reductase: a NH2Y731/R411A-α mutant unmasks a new conformation of the pathway residue 731† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c5sc03460d

J. Stubbe, M. Bennati, Müge Kasanmascheff, 2015, Chemical science.

Characterization of Y122F R2 of Escherichia coli ribonucleotide reductase by time-resolved physical biochemical methods and X-ray crystallography.

J. Tainer, J. Stubbe, A. Arvai, 1998, Biochemistry.

Identification of an active site residue of the R1 subunit of ribonucleotide reductase from Escherichia coli: characterization of substrate-induced polypeptide cleavage by C225SR1.

K. Biemann, J. Kyte, J. Stubbe, 1996, Biochemistry.

Circular Dichroism and Magnetic Circular Dichroism Studies of the Fully Reduced Binuclear Non-Heme Iron Active Site in the Escherichia coli R2 Subunit of Ribonucleoside Diphosphate Reductase

Edward I. Solomon, J. Martin Bollinger, JoAnne Stubbe, 1995 .

Mechanism of Assembly of the Tyrosyl Radical-Diiron(III) Cofactor of E. Coli Ribonucleotide Reductase: 1. Moessbauer Characterization of the Diferric Radical Precursor

J. Martin Bollinger, Natarajan Ravi, JoAnne Stubbe, 1994 .

EXAFS Studies of the B2 Subunit of the Ribonucleotide Reductase from E. coli

L. Que, J. Stubbe, M. Maroney, 1986 .

Lipases provide a new mechanistic model for polyhydroxybutyrate (PHB) synthases: characterization of the functional residues in Chromatium vinosum PHB synthase.

A. Sinskey, J. Stubbe, T. J. Kappock, 2000, Biochemistry.

PHA synthase from chromatium vinosum: cysteine 149 is involved in covalent catalysis.

William Arbuthnot Sir Lane, A. Sinskey, J. Stubbe, 1999, Biochemistry.

Growth and Localization of Polyhydroxybutyrate Granules in Ralstonia eutropha

G. Jensen, M. Beeby, J. Stubbe, 2011, Journal of bacteriology.

and Grant J . eutropha Polyhydroxybutyrate Granules in Ralstonia Growth and Localization of

M. Beeby, J. Stubbe, Mimi Cho, 2012 .

Kinetic Studies of Polyhydroxybutyrate Granule Formation in Wautersia eutropha H16 by Transmission Electron Microscopy

A. Sinskey, J. Stubbe, Jiamin Tian, 2005, Journal of bacteriology.

Analysis of Transient Polyhydroxybutyrate Production in Wautersia eutropha H16 by Quantitative Western Analysis and Transmission Electron Microscopy

A. Sinskey, J. Stubbe, N. Watson, 2005, Journal of bacteriology.

Transmission Electron Microscopy Quantitative Western Analysis and H 16 by Wautersia eutropha Production in Analysis of Transient Polyhydroxybutyrate

A. Sinskey, J. Stubbe, N. Watson, 2005 .

Photochemical Rescue of a Conformationally Inactivated Ribonucleotide Reductase.

D. Nocera, J. Stubbe, Brandon L. Greene, 2018, Journal of the American Chemical Society.

Properties of Site-Specifically Incorporated 3-Aminotyrosine in Proteins to Study Redox-Active Tyrosines: E. coli Ribonucleotide Reductase as a Paradigm

C. Tommos, D. Nocera, J. Stubbe, 2018 .

Generation of a stable, aminotyrosyl radical-induced α2β2 complex of Escherichia coli class Ia ribonucleotide reductase

F. Asturias, E. Brignole, D. Nocera, 2013, Proceedings of the National Academy of Sciences.

Mapping the subunit interface of ribonucleotide reductase (RNR) using photo cross-linking.

J. Stubbe, A. Q. Hassan, 2008, Bioorganic & medicinal chemistry letters.

PELDOR spectroscopy with DOPA-beta2 and NH2Y-alpha2s: distance measurements between residues involved in the radical propagation pathway of E. coli ribonucleotide reductase.

Clement T Y Chan, J. Stubbe, M. Bennati, 2007, Journal of the American Chemical Society.

Subunit Interaction Dynamics of Class Ia Ribonucleotide Reductases: In Search of a Robust Assay.

D. Nocera, J. Stubbe, K. Ravichandran, 2020, Biochemistry.

Use of 2,3,5-F 3 Y- β 2 and 3-NH 2 Y- α 2 to study PCET in E. coli Ribonucleotide Reductase

J. Stubbe, M. Seyedsayamdost, C. S. Yee, 2011 .

Use of 2,3,5-F[subscript 3]Y-beta 2 and 3-NH[subscript 2]Y-alpha 2 To Study Proton-Coupled Electron Transfer in Escherichia coli Ribonucleotide Reductase

J. Stubbe, M. Seyedsayamdost, C. S. Yee, 2010 .

EXAFS Studies of the B2 Subunit of the Ribonucleotide Reductase from E. coli.

L. Que, J. Stubbe, M. Maroney, 1987 .

Redox-linked changes to the hydrogen-bonding network of ribonucleotide reductase β2.

J. Stubbe, A. Offenbacher, B. Barry, 2013, Journal of the American Chemical Society.

Structure of the yeast ribonucleotide reductase Y2Y4 heterodimer

A. Rosenzweig, J. Stubbe, D. Perlstein, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Structure of the Catalytic Domain of the Class I Polyhydroxybutyrate Synthase from Cupriavidus necator*

J. Stubbe, M. Jost, C. Drennan, 2016, The Journal of Biological Chemistry.

Degradation of DNA-RNA hybrids by bleomycin: evidence for DNA strand specificity and for possible structural modulation of chemical mechanism

D. Vanderwall, J. Stubbe, J. Kozarich, 1988 .

Generation of the R2 subunit of ribonucleotide reductase by intein chemistry: insertion of 3-nitrotyrosine at residue 356 as a probe of the radical initiation process.

D. Nocera, J. Stubbe, M. Seyedsayamdost, 2003, Biochemistry.

Site-specific replacement of a conserved tyrosine in ribonucleotide reductase with an aniline amino acid: a mechanistic probe for a redox-active tyrosine.

D. Nocera, J. Stubbe, C. S. Yee, 2004, Journal of the American Chemical Society.

Christian R. Raetz (1946–2011)

J. Stubbe, 2012 .

Chris Raetz, scientist and enduring friend

J. Stubbe, W. Wickner, W. Dowhan, 2011, Proceedings of the National Academy of Sciences.

The Two Faces of SAM

J. Stubbe, 2011, Science.

Ribonucleotide Synthetase Mutants Defective in Aminoimidazole Serovar Typhimurium Salmonella enterica Altered Pathway Routing in a Class of

J. Stubbe, D. Downs, J. Zilles, 2014 .

Altered Pathway Routing in a Class ofSalmonella enterica Serovar Typhimurium Mutants Defective in Aminoimidazole Ribonucleotide Synthetase

J. Stubbe, D. Downs, J. Zilles, 2001, Journal of bacteriology.

Modulation of Phenol Oxidation in Cofacial Dyads.

D. Nocera, J. Stubbe, Robert L. Halbach, 2015, Journal of the American Chemical Society.

EPR distance measurements support a model for long-range radical initiation in E. coli ribonucleotide reductase.

J. Freed, P. Borbat, J. Stubbe, 2005, Journal of the American Chemical Society.

Synthase inAlcaligenes eutrophus H16:Localization ofthe Synthase EnzymeattheSurface ofPHB Granules

J. Stubbe, P. Reilly, 1993 .

Radical Transport Facilitated by a Proton Transfer Network at the Subunit Interface of Ribonucleotide Reductase.

D. Nocera, J. Stubbe, C. Drennan, 2023, Journal of the American Chemical Society.

Convergent allostery in ribonucleotide reductase

James Z. Chen, J. Bacik, W. Thomas, 2018, bioRxiv.

Conformationally Dynamic Radical Transfer within Ribonucleotide Reductase.

D. Nocera, J. Stubbe, Brandon L. Greene, 2017, Journal of the American Chemical Society.

Re(bpy)(CO)[subscript 3]CN as a Probe of Conformational Flexibility in a Photochemical Ribonucleotide Reductase

D. Nocera, Steven Y. Reece, J. Stubbe, 2009 .

RAPID FREEZE-QUENCH ENDOR OF THE RADICAL X INTERMEDIATE OF ESCHERICHIA COLI RIBONUCLEOTIDE REDUCTASE USING 17O2, H217O, AND 2H2O

J. Stubbe, B. Hoffman, W. Tong, 1996 .

Re(bpy)(CO)3CN as a probe of conformational flexibility in a photochemical ribonucleotide reductase.

D. Nocera, Steven Y. Reece, J. Stubbe, 2009, Biochemistry.

Electron transfer reactions of fluorotyrosyl radicals.

D. Nocera, Steven Y. Reece, J. Stubbe, 2006, Journal of the American Chemical Society.

Forward and reverse electron transfer with the Y356DOPA-beta2 heterodimer of E. coli ribonucleotide reductase.

J. Stubbe, M. Seyedsayamdost, 2007, Journal of the American Chemical Society.

Bleomycins: A Structural Model for Specificity, Binding, and Double Strand Cleavage

D. Vanderwall, Wei Wu, J. Stubbe, 2010 .

Discovery of a New Class I Ribonucleotide Reductase with an Essential DOPA Radical and NO Metal as an Initiator of Long-Range Radical Transfer.

J. Stubbe, M. Seyedsayamdost, 2018, Biochemistry.

Radical Transfer in E . Coli Ribonucleotide Reductase : a NHY / RA-Mutant Unmasks a New Conformation of the Pathway Residue 731

J. Stubbe, M. Bennati, Müge Kasanmascheff, 2016 .

Binding of Cob(II)alamin to the Adenosylcobalamin-dependent Ribonucleotide Reductase fromLactobacillus leichmannii

J. Stubbe, G. Gerfen, V. Samano, 1999, The Journal of Biological Chemistry.

Protein structure. Controlling radical reactions.

J. Stubbe, 1994, Nature.

Pulsed ELDOR spectroscopy measures the distance between the two tyrosyl dadicals in the R2 subunit of the E. coli ribonucleotide reductase.

J. Stubbe, M. Bennati, J. Antonic, 2003, Journal of the American Chemical Society.

Equilibration of Tyrosyl Radicals (Y[• over 356], Y[• over 731], Y[• over 730]) in the Radical Propagation Pathway of the Escherichia coli Class Ia Ribonucleotide Reductase

R. Griffin, K. Yokoyama, J. Stubbe, 2011 .

Incorporation of 18O into glycolic acid obtained from the bleomycin-mediated degradation of DNA. Evidence for 4'-radical trapping by 18O2

G. Mcgall, J. Stubbe, J. Kozarich, 1987 .

Inactivation of Lactobacillus leichmannii ribonucleotide reductase by 2',2'-difluoro-2'-deoxycytidine 5'-triphosphate: adenosylcobalamin destruction and formation of a nucleotide-based radical.

J. Stubbe, G. Gerfen, G. Lohman, 2010, Biochemistry.

Enolase catalyzed beta,gamma-alpha,beta isomerization of 2-phospho-3-butenoic acid to (Z)-phosphoenol-alpha-ketobutyrate.

J. Stubbe, J. Appelbaum, 1975, Biochemistry.

Sequence-specific double-strand cleavage of DNA by Fe-bleomycin. 1. The detection of sequence-specific double-strand breaks using hairpin oligonucleotides.

M. Absalon, J. Stubbe, J. Kozarich, 1995, Biochemistry.

2'-Azido-2'-deoxynucleotide interaction with E. coli ribonucleotide reductase: generation of a new radical species

JoAnne Stubbe, Morris J. Robins, J. Stubbe, 1984 .

Christian Raetz: scientist and friend extraordinaire.

H. Nikaido, J. Stubbe, W. Wickner, 2013, Annual review of biochemistry.

Detection of covalent and noncovalent intermediates in the polymerization reaction catalyzed by a C149S class III polyhydroxybutyrate synthase.

J. Stubbe, S. Chakraborty, Ping Li, 2009, Biochemistry.

DIRECT EPR SPECTROSCOPIC EVIDENCE FOR AN ALLYLIC RADICAL GENERATED FROM (E)-2'-FLUOROMETHYLENE-2'-DEOXYCYTIDINE 5'-DIPHOSPHATE BY E. COLI RIBONUCLEOTI DE REDUCTASE

J. Stubbe, G. Gerfen, W. Donk, 1998 .

Ribonucleotide Reductase: Recent Advances

J. Stubbe, J. Cotruvo, 2008 .

Structural Basis for Activation of Class Ib Ribonucleotide Reductase

A. Rosenzweig, J. Stubbe, J. Cotruvo, 2010, Science.

Dif1 is a DNA-damage-regulated facilitator of nuclear import for ribonucleotide reductase.

S. Elledge, J. Stubbe, Jun Wang, 2008, Molecular cell.

Determination of the in vivo stoichiometry of tyrosyl radical per betabeta' in Saccharomyces cerevisiae ribonucleotide reductase.

J. Stubbe, Deborah L. Perlstein, Mingxia Huang, 2006, Biochemistry.

J. Stubbe, J. Cotruvo, T. A. Stich, 2013, Journal of the American Chemical Society.

An active dimanganese(III)-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase.

J. Stubbe, J. Cotruvo, 2010, Biochemistry.

Metallation and mismetallation of iron and manganese proteins in vitro and in vivo: the class I ribonucleotide reductases as a case study.

J. Stubbe, J. Cotruvo, 2012, Metallomics : integrated biometal science.

Structural interconversions modulate activity of Escherichia coli ribonucleotide reductase

F. Asturias, K. Yokoyama, E. Brignole, 2011, Proceedings of the National Academy of Sciences of the United States of America.

Properties of Site-Specifically Incorporated 3-Aminotyrosine in Proteins To Study Redox-Active Tyrosines: Escherichia coli Ribonucleotide Reductase as a Paradigm.

C. Tommos, D. Nocera, J. Stubbe, 2018, Biochemistry.

Equilibration of tyrosyl radicals (Y356•, Y731•, Y730•) in the radical propagation pathway of the Escherichia coli class Ia ribonucleotide reductase.

R. Griffin, K. Yokoyama, J. Stubbe, 2011, Journal of the American Chemical Society.

The class III ribonucleotide reductase from Neisseria bacilliformis can utilize thioredoxin as a reductant

J. Stubbe, C. Drennan, Jiyeon Baek, 2014, Proceedings of the National Academy of Sciences.

Radical transfer in E. coli ribonucleotide reductase: a NH2Y731/R411A-α mutant unmasks a new conformation of the pathway residue 731

J. Stubbe, M. Bennati, Müge Kasanmascheff, 2015, Chemical science.

ENDOR spectroscopy and DFT calculations: evidence for the hydrogen-bond network within α2 in the PCET of E. coli ribonucleotide reductase.

F. Neese, J. Stubbe, M. Bennati, 2012, Journal of the American Chemical Society.

A >200 meV Uphill Thermodynamic Landscape for Radical Transport in Escherichia coli Ribonucleotide Reductase Determined Using Fluorotyrosine-Substituted Enzymes

C. Tommos, D. Nocera, J. Stubbe, 2016, Journal of the American Chemical Society.

Modulation of Phenol Oxidation in Cofacial Dyads.

D. Nocera, J. Stubbe, Robert L. Halbach, 2015, Journal of the American Chemical Society.

Deciphering radical transport in the large subunit of class I ribonucleotide reductase.

D. Nocera, J. Stubbe, B. Anderson, 2011, Journal of the American Chemical Society.

Insight into the mechanism of inactivation of ribonucleotide reductase by gemcitabine 5'-diphosphate in the presence or absence of reductant.

R. Griffin, K. Yokoyama, J. Stubbe, 2009, Biochemistry.

PET Polymer Recycling.

J. Stubbe, M. O’Reilly, 2020, Biochemistry.

Clofarabine targets the large subunit (α) of human ribonucleotide reductase in live cells by assembly into persistent hexamers.

F. Asturias, E. Brignole, J. Stubbe, 2012, Chemistry & biology.