D. Dean

发表

Feedback regulation of ribosomal protein gene expression in Escherichia coli: structural homology of ribosomal RNA and ribosomal protein MRNA.

M. Nomura, J. Yates, L. Post, 1980, Proceedings of the National Academy of Sciences of the United States of America.

Biosynthesis of the nitrogenase iron-molybdenum-cofactor from Azotobacter vinelandii.

J. Frazzon, D. Dean, 2002, Metal ions in biological systems.

Controlled Expression and Functional Analysis of Iron-Sulfur Cluster Biosynthetic Components within Azotobacter vinelandii

D. Dean, Deborah C. Johnson, M. Unciuleac, 2006, Journal of bacteriology.

A Proposed Role for the Azotobacter vinelandii NfuA Protein as an Intermediate Iron-Sulfur Cluster Carrier*

Sibali Bandyopadhyay, D. Dean, S. Naik, 2008, Journal of Biological Chemistry.

Transcriptional Profiling of Nitrogen Fixation in Azotobacter vinelandii

J. W. Peters, J. Setubal, E. Boyd, 2011, Journal of bacteriology.

Structure, function, and formation of biological iron-sulfur clusters.

D. Dean, Deborah C. Johnson, Michael K. Johnson, 2005, Annual review of biochemistry.

Catalytic formation of a nitrogenase iron-sulfur cluster.

D. Dean, L. Zheng, Limin Zheng, 1994, The Journal of biological chemistry.

IscA, an alternate scaffold for Fe-S cluster biosynthesis.

C. Krebs, J. Agar, J. Frazzon, 2001, Biochemistry.

Carbon dioxide reduction to methane and coupling with acetylene to form propylene catalyzed by remodeled nitrogenase

L. Seefeldt, D. Dean, Zhi-Yong Yang, 2012, Proceedings of the National Academy of Sciences.

Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product.

R. White, D. Dean, L. Zheng, 1994, Biochemistry.

IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU.

C. Krebs, J. Agar, J. Frazzon, 2000, Biochemistry.

Azotobacter vinelandii nifD- and nifE-encoded polypeptides share structural homology.

D. Dean, K. Brigle, 1985, Proceedings of the National Academy of Sciences of the United States of America.

Products of the iron-molybdenum cofactor-specific biosynthetic genes, nifE and nifN, are structurally homologous to the products of the nitrogenase molybdenum-iron protein genes, nifD and nifK

M. Weiss, W. Newton, D. Dean, 1987, Journal of bacteriology.

Characteristics of NIFNE in Azotobacter vinelandii Strains

G. Roberts, D. Dean, V. K. Shah, 1995, The Journal of Biological Chemistry.

Mechanism of Mo-dependent nitrogenase.

L. Seefeldt, B. Hoffman, D. Dean, 2009, Annual review of biochemistry.

Electron transfer in nitrogenase catalysis.

L. Seefeldt, B. Hoffman, D. Dean, 2012, Current opinion in chemical biology.

Nitrogenase: a draft mechanism.

L. Seefeldt, B. Hoffman, D. Dean, 2013, Accounts of chemical research.

Molybdenum Nitrogenase Catalyzes the Reduction and Coupling of CO to Form Hydrocarbons*♦

L. Seefeldt, D. Dean, Zhi-Yong Yang, 2011, The Journal of Biological Chemistry.

In vivo iron–sulfur cluster formation

D. Dean, M. Unciuleac, I. O'Carroll, 2008, Proceedings of the National Academy of Sciences.

Conformational gating of electron transfer from the nitrogenase Fe protein to MoFe protein.

L. Seefeldt, B. Hoffman, Karamatullah Danyal, 2010, Journal of the American Chemical Society.

Formation and insertion of the nitrogenase iron-molybdenum cofactor.

Yilin Hu, M. Ribbe, D. Dean, 2004, Chemical reviews.

Catalytic Mechanism of Sep-tRNA:Cys-tRNA Synthase

D. Söll, Yuchen Liu, R. Orlando, 2011, The Journal of Biological Chemistry.

Energy Transduction in Nitrogenase.

J. W. Peters, D. Beratan, L. Seefeldt, 2018, Accounts of chemical research.

Exploring Electron/Proton Transfer and Conformational Changes in the Nitrogenase MoFe Protein and FeMo-cofactor Through Cryoreduction/EPR Measurements.

A. Fielding, L. Seefeldt, B. Hoffman, 2016, Israel journal of chemistry.

Evidence That the Pi Release Event Is the Rate-Limiting Step in the Nitrogenase Catalytic Cycle.

J. W. Peters, Rhesa N Ledbetter, L. Seefeldt, 2016, Biochemistry.

Temperature invariance of the nitrogenase electron transfer mechanism.

L. Seefeldt, B. Hoffman, Karamatullah Danyal, 2012, Biochemistry.

Catalytic and biophysical properties of a nitrogenase Apo-MoFe protein produced by a nifB-deletion mutant of Azotobacter vinelandii.

W. Lanzilotta, L. Seefeldt, D. Dean, 1998, Biochemistry.

Reductive Elimination of H2 Activates Nitrogenase to Reduce the N≡N Triple Bond: Characterization of the E4(4H) Janus Intermediate in Wild-Type Enzyme.

L. Seefeldt, B. Hoffman, D. Dean, 2016, Journal of the American Chemical Society.

57Fe ENDOR spectroscopy and 'electron inventory' analysis of the nitrogenase E4 intermediate suggest the metal-ion core of FeMo-cofactor cycles through only one redox couple.

L. Seefeldt, B. Hoffman, J. Telser, 2011, Journal of the American Chemical Society.

Trapping an intermediate of dinitrogen (N2) reduction on nitrogenase.

L. Seefeldt, B. Hoffman, B. M. Barney, 2009, Biochemistry.

Trapping a hydrazine reduction intermediate on the nitrogenase active site.

L. Seefeldt, B. Hoffman, Hong-In Lee, 2005, Biochemistry.

Trapping H- bound to the nitrogenase FeMo-cofactor active site during H2 evolution: characterization by ENDOR spectroscopy.

L. Seefeldt, B. Hoffman, Hong-In Lee, 2005, Journal of the American Chemical Society.

Substrate Interaction at an Iron-Sulfur Face of the FeMo-cofactor during Nitrogenase Catalysis*

L. Seefeldt, B. M. Barney, D. Dean, 2004, Journal of Biological Chemistry.

Electrocatalytic CO2 reduction catalyzed by nitrogenase MoFe and FeFe proteins.

T. L. Liu, L. Seefeldt, D. Dean, 2018, Bioelectrochemistry.

FeS Cluster Assembly: NIF System in Nitrogen‐Fixing Bacteria

D. Dean, P. D. Santos, 2017 .

Photoinduced Reductive Elimination of H2 from the Nitrogenase Dihydride (Janus) State Involves a FeMo-cofactor-H2 Intermediate.

L. Seefeldt, B. Hoffman, D. Dean, 2017, Inorganic chemistry.

Reversible Photoinduced Reductive Elimination of H2 from the Nitrogenase Dihydride State, the E(4)(4H) Janus Intermediate.

L. Seefeldt, B. Hoffman, D. Dean, 2016, Journal of the American Chemical Society.

Identification of a key catalytic intermediate demonstrates that nitrogenase is activated by the reversible exchange of N₂ for H₂.

L. Seefeldt, B. Hoffman, D. Dean, 2015, Journal of the American Chemical Society.

On reversible H2 loss upon N2 binding to FeMo-cofactor of nitrogenase

L. Seefeldt, B. Hoffman, D. Dean, 2013, Proceedings of the National Academy of Sciences.

Nitrogenase reduction of carbon-containing compounds.

L. Seefeldt, S. Duval, D. Dean, 2013, Biochimica et biophysica acta.

Unification of reaction pathway and kinetic scheme for N2 reduction catalyzed by nitrogenase

L. Seefeldt, B. Hoffman, B. M. Barney, 2012, Proceedings of the National Academy of Sciences.

ENDOR/HYSCORE studies of the common intermediate trapped during nitrogenase reduction of N2H2, CH3N2H, and N2H4 support an alternating reaction pathway for N2 reduction.

L. Seefeldt, B. Hoffman, S. Dikanov, 2011, Journal of the American Chemical Society.

Is Mo involved in hydride binding by the four-electron reduced (E4) intermediate of the nitrogenase MoFe protein?

L. Seefeldt, B. Hoffman, D. Dean, 2010, Journal of the American Chemical Society.

Climbing nitrogenase: toward a mechanism of enzymatic nitrogen fixation.

L. Seefeldt, B. Hoffman, D. Dean, 2009, Accounts of chemical research.

Alkyne substrate interaction within the nitrogenase MoFe protein.

L. Seefeldt, B. M. Barney, D. Dean, 2007, Journal of inorganic biochemistry.

Connecting nitrogenase intermediates with the kinetic scheme for N2 reduction by a relaxation protocol and identification of the N2 binding state

L. Seefeldt, B. Hoffman, B. M. Barney, 2007, Proceedings of the National Academy of Sciences.

Substrate interactions with the nitrogenase active site.

L. Seefeldt, B. Hoffman, Hong-In Lee, 2005, Accounts of chemical research.

An organometallic intermediate during alkyne reduction by nitrogenase.

L. Seefeldt, B. Hoffman, Hong-In Lee, 2004, Journal of the American Chemical Society.

Breaking the N2 triple bond: insights into the nitrogenase mechanism.

L. Seefeldt, B. Hoffman, Hong-In Lee, 2006, Dalton transactions.

Substrate interactions with nitrogenase: Fe versus Mo.

L. Seefeldt, D. Dean, I. Dance, 2004, Biochemistry.

Strategies for the Functional Analysis of the Azotobacter Vinelandii MoFe Protein and its Active Site FeMo-Cofactor

L. Seefeldt, D. Dean, P. D. Santos, 2004 .

Mo-, V-, and Fe-Nitrogenases Use a Universal Eight-Electron Reductive-Elimination Mechanism to Achieve N2 Reduction.

N. Kelleher, L. Seefeldt, B. Hoffman, 2019, Biochemistry.

Identification of a nitrogenase protein-protein interaction site defined by residues 59 through 67 within the Azotobacter vinelandii Fe protein.

J. W. Peters, K. Fisher, D. Dean, 1994, The Journal of biological chemistry.

Application of affinity purification methods for analysis of the nitrogenase system from Azotobacter vinelandii.

L. Seefeldt, Julia S. Martín del Campo, D. Dean, 2018, Methods in enzymology.

Uncoupling nitrogenase: catalytic reduction of hydrazine to ammonia by a MoFe protein in the absence of Fe protein-ATP.

F. Armstrong, L. Seefeldt, B. Hoffman, 2010, Journal of the American Chemical Society.

The One-Electron Reduced Active-Site FeFe-Cofactor of Fe-Nitrogenase Contains a Hydride Bound to a Formally Oxidized Metal-Ion Core.

L. Seefeldt, B. Hoffman, D. Dean, 2022, Inorganic chemistry.

CO as a substrate and inhibitor of H+ reduction for the Mo-, V-, and Fe-nitrogenase isozymes.

L. Seefeldt, B. Hoffman, D. Dean, 2020, Journal of inorganic biochemistry.

The NifZ accessory protein has an equivalent function in maturation of both nitrogenase MoFe protein P-clusters

L. Seefeldt, Julia S. Martín del Campo, D. Dean, 2019, The Journal of Biological Chemistry.

Sequential and differential interaction of assembly factors during nitrogenase MoFe protein maturation

L. Seefeldt, W. K. Ray, D. Dean, 2018, The Journal of Biological Chemistry.

Nitrogenase bioelectrocatalysis: heterogeneous ammonia and hydrogen production by MoFe protein

Ross D. Milton, L. Seefeldt, S. Minteer, 2016 .

EXAFS and NRVS reveal a conformational distortion of the FeMo-cofactor in the MoFe nitrogenase propargyl alcohol complex.

L. Seefeldt, S. George, S. Cramer, 2012, Journal of inorganic biochemistry.

Steric control of the Hi-CO MoFe nitrogenase complex revealed by stopped-flow infrared spectroscopy.

L. Seefeldt, S. George, S. Cramer, 2011, Angewandte Chemie.

Transcriptional Proﬁling of Nitrogen Fixation in Azotobacter vinelandii (cid:1)

J. W. Peters, J. Setubal, E. Boyd, 2011 .

Testing if the interstitial atom, X, of the nitrogenase molybdenum-iron cofactor is N or C: ENDOR, ESEEM, and DFT studies of the S = 3/2 resting state in multiple environments.

D. Case, L. Seefeldt, B. Hoffman, 2007, Inorganic chemistry.

Diazene (HN=NH) is a substrate for nitrogenase: insights into the pathway of N2 reduction.

L. Seefeldt, B. Hoffman, B. M. Barney, 2007, Biochemistry.

A methyldiazene (HNNCH3)-derived species bound to the nitrogenase active-site FeMo cofactor: Implications for mechanism

L. Seefeldt, B. Hoffman, B. M. Barney, 2006, Proceedings of the National Academy of Sciences.

Electron inventory, kinetic assignment (E(n)), structure, and bonding of nitrogenase turnover intermediates with C2H2 and CO.

B. Hoffman, M. Sørlie, Hong-In Lee, 2005, Journal of the American Chemical Society.

Intermediates Trapped during Nitrogenase Reduction of N⋮N, CH3−NNH, and H2N−NH2

L. Seefeldt, B. Hoffman, Hong-In Lee, 2005 .

The interstitial atom of the nitrogenase FeMo-cofactor: ENDOR and ESEEM evidence that it is not a nitrogen.

L. Seefeldt, B. Hoffman, Hong-In Lee, 2005, Journal of the American Chemical Society.

Localization of a Catalytic Intermediate Bound to the FeMo-cofactor of Nitrogenase*

L. Seefeldt, D. Dean, P. D. Dos Santos, 2004, Journal of Biological Chemistry.

Localization of a substrate binding site on the FeMo-cofactor in nitrogenase: trapping propargyl alcohol with an alpha-70-substituted MoFe protein.

L. Seefeldt, B. Hoffman, D. Dean, 2003, Biochemistry.

The interstitial atom of the nitrogenase FeMo-cofactor: ENDOR and ESEEM show it is not an exchangeable nitrogen.

L. Seefeldt, B. Hoffman, Hong-In Lee, 2003, Journal of the American Chemical Society.

Interaction of acetylene and cyanide with the resting state of nitrogenase alpha-96-substituted MoFe proteins.

L. Seefeldt, B. Hoffman, D. Dean, 2001, Biochemistry.

Isolation and Characterization of an Acetylene-resistant Nitrogenase*

L. Seefeldt, D. Dean, V. Cash, 2000, The Journal of Biological Chemistry.

Spectroscopic evidence for changes in the redox state of the nitrogenase P-cluster during turnover.

L. Seefeldt, D. Dean, J. M. Chan, 1999, Biochemistry.

Evidence for coupled electron and proton transfer in the [8Fe-7S] cluster of nitrogenase.

W. Lanzilotta, L. Seefeldt, D. Dean, 1998, Biochemistry.

Involvement of the P Cluster in Intramolecular Electron Transfer within the Nitrogenase MoFe Protein (*)

J. W. Peters, K. Fisher, W. Newton, 1995, The Journal of Biological Chemistry.

Role of the MoFe protein alpha-subunit histidine-195 residue in FeMo-cofactor binding and nitrogenase catalysis.

C. H. Kim, C. H. Kim, W. Newton, 1995, Biochemistry.

N coordination of FeMo cofactor requires His-195 of the MoFe protein alpha subunit and is essential for biological nitrogen fixation.

W. Newton, D. Dean, H. Thomann, 1991, Proceedings of the National Academy of Sciences of the United States of America.

Role for the nitrogenase MoFe protein α-subunit in FeMo-cofactor binding and catalysis

H. May, W. Newton, D. Dean, 1990, Nature.

Construction and characterization of an Azotobacter vinelandii strain with mutations in the genes encoding flavodoxin and ferredoxin I

S. Iismaa, B. Burgess, D. Dean, 1989, Journal of bacteriology.

Light-driven carbon dioxide reduction to methane by nitrogenase in a photosynthetic bacterium

Yanning Zheng, L. Seefeldt, C. Harwood, 2016, Proceedings of the National Academy of Sciences.

Activity, reconstitution, and accumulation of nitrogenase components in Azotobacter vinelandii mutant strains containing defined deletions within the nitrogenase structural gene cluster

B. Burgess, D. Dean, A. Robinson, 1986, Journal of bacteriology.

AnfO controls fidelity of nitrogenase FeFe protein maturation by preventing misincorporation of FeV‐cofactor

L. Seefeldt, D. Dean, A. Pérez-González, 2022, Molecular microbiology.

Isolation, sequencing, and mutagenesis of the nifF gene encoding flavodoxin from Azotobacter vinelandii.

D. Dean, M. Jacobson, L. T. Bennett, 1988, The Journal of biological chemistry.

Evidence for multiple substrate-reduction sites and distinct inhibitor-binding sites from an altered Azotobacter vinelandii nitrogenase MoFe protein.

W. Newton, D. Dean, J. Shen, 1997, Biochemistry.

Nitrogen Fixation by Azotobacter vinelandii Strains Having Deletions in Structural Genes for Nitrogenase

D. Dean, M. Jacobson, R. Premakumar, 1986, Science.

CHAPTER 5 – Use of Short-Chain Alkynes to Locate the Nitrogenase Catalytic Site

L. Seefeldt, D. Dean, P. D. Santos, 2002 .

14N electron spin-echo envelope modulation of the S = 3/2 spin system of the Azotobacter vinelandii nitrogenase iron-molybdenum cofactor.

B. Hoffman, W. Newton, D. Dean, 1998, Biochemistry.

Ionic interactions in the nitrogenase complex. Properties of Fe-protein containing substitutions for Arg-100.

J. Howard, C. Kim, D. Wolle, 1992, The Journal of biological chemistry.

Mapping the site(s) of MgATP and MgADP interaction with the nitrogenase of Azotobacter vinelandii. Lysine 15 of the iron protein plays a major role in MgATP interaction.

L. Seefeldt, D. Dean, L. Mortenson, 1992, The Journal of biological chemistry.

Fe:S cluster ligands are the only cysteines required for nitrogenase Fe-protein activities.

J. Howard, D. Dean, R. Davis, 1989, The Journal of biological chemistry.

Characterization of an Intermediate in the Reduction of Acetylene by the Nitrogenase α-Gln195 MoFe Protein by Q-band EPR and 13C,1H ENDOR

B. Hoffman, M. Sørlie, Hong-In Lee, 2000 .

A conformational role for NifW in the maturation of molybdenum nitrogenase P-cluster

L. Seefeldt, S. DeBeer, D. Dean, 2022, Chemical science.

Kinetic Understanding of N2 Reduction versus H2 Evolution at the E4(4H) Janus State in the Three Nitrogenases.

L. Seefeldt, B. Hoffman, D. Dean, 2018, Biochemistry.

The electronic structure of FeV-cofactor in vanadium-dependent nitrogenase†

L. Seefeldt, B. Hoffman, Julia S. Martín del Campo, 2021, Chemical science.

Stereospecificity of acetylene reduction catalyzed by nitrogenase.

L. Seefeldt, D. Dean, J. Christiansen, 2001, Journal of the American Chemical Society.

DETECTION OF A NEW RADICAL AND FEMO-COFACTOR EPR SIGNAL DURING ACETYLENE REDUCTION BY THE ALPHA -H195Q MUTANT OF NITROGENASE

M. Sørlie, D. Dean, B. Hales, 1999 .

Nitrogenase-catalyzed ethane production and CO-sensitive hydrogen evolution from MoFe proteins having amino acid substitutions in an alpha-subunit FeMo cofactor-binding domain.

W. Newton, D. Dean, D. Scott, 1992, The Journal of biological chemistry.

Time-Resolved EPR Study of H2 Reductive Elimination from the Photoexcited Nitrogenase Janus E4(4H) Intermediate.

M. Wasielewski, L. Seefeldt, B. Hoffman, 2019, Journal of Physical Chemistry B.

Hydride Conformers of the Nitrogenase FeMo-cofactor Two-Electron Reduced State E2(2H), Assigned Using Cryogenic Intra Electron Paramagnetic Resonance Cavity Photolysis

L. Seefeldt, B. Hoffman, D. Dean, 2018, Inorganic chemistry.

Mechanism of N2 Reduction Catalyzed by Fe-Nitrogenase Involves Reductive Elimination of H2.

N. Kelleher, L. Seefeldt, B. Hoffman, 2017, Biochemistry.

Electron Redistribution within the Nitrogenase Active Site FeMo-Cofactor During Reductive Elimination of H2 to Achieve N≡N Triple-Bond Activation.

L. Seefeldt, B. Hoffman, D. Dean, 2020, Journal of the American Chemical Society.

Specificity of NifEN and VnfEN for the Assembly of Nitrogenase Active Site Cofactors in Azotobacter vinelandii

L. Seefeldt, O. Einsle, D. Dean, 2021, mBio.

NifX and NifEN exchange NifB cofactor and the VK‐cluster, a newly isolated intermediate of the iron‐molybdenum cofactor biosynthetic pathway

L. Curatti, P. Ludden, D. Dean, 2007, Molecular microbiology.

Iron-Sulfur Cluster Assembly

J. Frazzon, D. Dean, Michael K. Johnson, 2004, Journal of Biological Chemistry.

Inhibition of Iron-Molybdenum Cofactor Biosynthesis by L127Δ NifH and Evidence for a Complex Formation between L127Δ NifH and NifNE*

M. J. Ryle, W. Lanzilotta, P. Ludden, 1999, The Journal of Biological Chemistry.

NifU and NifS are required for the maturation of nitrogenase and cannot replace the function of isc-gene products in Azotobacter vinelandii.

D. Dean, P. D. Dos Santos, D. Johnson, 2005, Biochemical Society transactions.

Construction and characterization of a heterodimeric iron protein: defining roles for adenosine triphosphate in nitrogenase catalysis.

L. Seefeldt, D. Dean, W. Wu, 2000, Biochemistry.

The Azotobacter vinelandii NifEN complex contains two identical [4Fe-4S] clusters.

J. Agar, G. Roberts, D. Dean, 1998, Biochemistry.

Purification of the Azotobacter vinelandii nifV-encoded homocitrate synthase

R. White, D. Dean, L. Zheng, 1997, Journal of bacteriology.

Nucleotide sequence and mutagenesis of the nifA gene from Azotobacter vinelandii

F. Cannon, D. Dean, L. T. Bennett, 1988, Molecular microbiology.

Electron spin echo envelope modulation spectroscopic analysis of altered nitrogenase MoFe proteins from Azotobacter vinelandii.

C. H. Kim, V. DeRose, B. Hoffman, 1995, Biochemistry.

Evidence that conserved residues Cys‐62 and Cys‐154 within the Azotobacter vinelandii nitrogenase MoFe protein α‐subunit are essential for nitrogenase activity but conserved residues His‐83 and Cys‐88 are not

R. Setterquist, W. Newton, D. Dean, 1990, Molecular microbiology.

Site-directed mutagenesis of the nitrogenase MoFe protein of Azotobacter vinelandii.

R. Setterquist, M. Weiss, W. Newton, 1987, Proceedings of the National Academy of Sciences of the United States of America.

Iron-molybdenum cofactor biosynthesis in Azotobacter vinelandii requires the iron protein of nitrogenase.

B. Burgess, D. Dean, A. Robinson, 1987, The Journal of biological chemistry.

Q-Band ENDOR Studies of the Nitrogenase MoFe Protein under Turnover Conditions: Substrate-Inhibitor-Binding to and Metal-Ion Valencies of the FeMo-Cofactor

B. Hoffman, M. Sørlie, W. Orme-Johnson, 2003 .

Probing Catalytic Function through Amino-Acid Substitutions in Azotobacter Vinelandii Molybdenum-Dependent Nitrogenase

K. Fisher, Chul-Hwan Kim, W. Newton, 1995 .

Climbing nitrogenase: toward a mechanism of enzymatic nitrogen fixation.

L. Seefeldt, B. Hoffman, D. Dean, 2009, Accounts of chemical research.

Altered nitrogenase MoFe proteins from Azotobacter vinelandii. Analysis of MoFe proteins having amino acid substitutions for the conserved cysteine residues within the beta-subunit.

H. May, W. Newton, D. Dean, 1991, The Biochemical journal.

VnfY Is Required for Full Activity of the Vanadium-Containing Dinitrogenase in Azotobacter vinelandii

C. Rüttimann-Johnson, P. Ludden, D. Dean, 2003, Journal of bacteriology.

13C ENDOR Characterization of the Central Carbon within the Nitrogenase Catalytic Cofactor Indicates That the CFe6 Core Is a Stabilizing "Heart of Steel".

L. Seefeldt, B. Hoffman, D. Dean, 2022, Journal of the American Chemical Society.

Identification of FeMoco domains within the nitrogenase MoFe protein

W. Newton, D. Dean, D. Scott, 1990 .

Nitrogenase: Two Decades of Biochemical Genetics

J. Frazzon, D. Dean, J. Spee, 1997 .

Intermolecular Electron Transfer and Substrate Reduction Properties of MoFe Proteins Altered by Site-Specific Amino Acid Substitution

Chul-Hwan Kim, W. Newton, D. Dean, 1993 .

A hybrid Azotobacter vinelandii-Clostridium pasteurianum nitrogenase iron protein that has in vivo and in vitro catalytic activity.

D. Dean, M. Jacobson, J. Cantwell, 1990, The Journal of biological chemistry.

Physical and genetic map of the major nif gene cluster from Azotobacter vinelandii

R. Setterquist, J. Beynon, W. Newton, 1989, Journal of bacteriology.

nifU gene product from Azotobacter vinelandii is a homodimer that contains two identical [2Fe-2S] clusters.

D. Dean, M. Johnson, T. Morgan, 1994, Biochemistry.

Involvement of PLP in biological formation iron-sulfur clusters

D. Dean, Limin Zheng, 1994 .

Revised nucleotide sequence of the Azotobacter vinelandii nifE gene.

D. Dean, K. Brigle, 1988, Nucleic acids research.

Complete nucleotide sequence of the Azotobacter vinelandii nitrogenase structural gene cluster.

W. Newton, D. Dean, K. Brigle, 1985, Gene.

NifS-directed assembly of a transient [2Fe-2S] cluster within the NifU protein.

J. Agar, D. Dean, Michael K. Johnson, 2000, Proceedings of the National Academy of Sciences of the United States of America.

Chemistry and Biochemistry of Nitrogenase (Part 1)

D. Dean, R. Thorneley, 2000 .

Keeping the nitrogen-fixation dream alive

D. Dean, E. J. Vicente, 2017, Proceedings of the National Academy of Sciences.

The nifH, nifM and nifN genes of Azotobacter vinelandii: Characterisation by Tn5 mutagenesis and isolation from pLAFR1 gene banks

J. Ramos, D. Dean, C. Kennedy, 1986, Molecular and General Genetics MGG.

Gene dosage analysis in Azotobacter vinelandii.

A. Garzón, J. Casadesús, D. Dean, 1992, Genetics.

The N-terminal and C-terminal portions of NifV are encoded by two different genes in Clostridium pasteurianum

J. S. Chen, J. Johnson, D. Dean, 1991, Journal of bacteriology.

Role of NifS in maturation of glutamine phosphoribosylpyrophosphate amidotransferase

H. Zalkin, D. Dean, L. Zheng, 1997, Journal of bacteriology.

Negative cooperativity in the nitrogenase Fe protein electron delivery cycle

L. Seefeldt, E. Antony, B. Hoffman, 2016, Proceedings of the National Academy of Sciences.

Structure of a Cofactor-Deficient Nitrogenase MoFe Protein

D. Rees, O. Einsle, B. Burgess, 2002, Science.

A newly discovered role for iron-sulfur clusters

D. Dean, P. D. Dos Santos, 2008, Proceedings of the National Academy of Sciences.

Modular organization and identification of a mononuclear iron-binding site within the NifU protein

J. Agar, D. Dean, Michael K. Johnson, 2000, JBIC Journal of Biological Inorganic Chemistry.

Biosynthesis of iron-sulphur clusters is a complex and highly conserved process.

J. Frazzon, D. Dean, J. Fick, 2001, Biochemical Society transactions.

Evidence that conserved residues Cys-62 and Cys-154 within the Azotobacter vinelandii nitrogenase MoFe protein alpha-subunit are essential for nitrogenase activity but conserved residues His-83 and Cys-88 are not.

R. Setterquist, W. Newton, D. Dean, 1990, Molecular microbiology.

Nitrogenase structure and function: a biochemical-genetic perspective.

J. W. Peters, K. Fisher, D. Dean, 1995, Annual review of microbiology.

Alteration of the Bacillus subtilis glutamine synthetase results in overproduction of the enzyme

J. Hoch, A. Aronson, D. Dean, 1977, Journal of bacteriology.

Insights into substrate binding at FeMo-cofactor in nitrogenase from the structure of an alpha-70(Ile) MoFe protein variant.

J. W. Peters, L. Seefeldt, B. M. Barney, 2010, Journal of inorganic biochemistry.

MECHANISTIC FEATURES OF THE MO-CONTAINING NITROGENASE.

L. Seefeldt, D. Dean, J. Christiansen, 2001, Annual review of plant physiology and plant molecular biology.

A Confirmation of the Quench-Cryoannealing Relaxation Protocol for Identifying Reduction States of Freeze-Trapped Nitrogenase Intermediates

L. Seefeldt, B. Hoffman, Karamatullah Danyal, 2014, Inorganic chemistry.

Mechanism of Nitrogen Fixation by Nitrogenase: The Next Stage

Dennis R. Dean, Lance C. Seefeldt, L. Seefeldt, 2014, Chemical reviews.

Selection of Bacillus subtilis mutants impaired in ammonia assimilation

A. Aronson, D. Dean, 1980, Journal of bacteriology.

Crystal structure and functional studies of an unusual L-cysteine desulfurase from Archaeoglobus fulgidus.

J. Fontecilla-Camps, D. Dean, J. S. de Oliveira, 2012, Dalton transactions.

(IscS-IscU)2Complex Structures Provide Insights into Fe2S2Biogenesis and Transfer

P. Amara, J. Fontecilla-Camps, D. Dean, 2012 .

(IscS-IscU)2 complex structures provide insights into Fe2S2 biogenesis and transfer.

P. Amara, J. Fontecilla-Camps, D. Dean, 2012, Angewandte Chemie.

Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistry.

J. Frazzon, D. Dean, 2003, Current opinion in chemical biology.

Feedback regulation of iron-sulfur cluster biosynthesis

J. Frazzon, D. Dean, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Nitrite and Hydroxylamine as Nitrogenase Substrates: Mechanistic Implications for the Pathway of N2 Reduction

L. Seefeldt, B. Hoffman, Karamatullah Danyal, 2014, Journal of the American Chemical Society.

In vitro activation of apo-aconitase using a [4Fe-4S] cluster-loaded form of the IscU [Fe-S] cluster scaffolding protein.

D. Dean, M. Unciuleac, S. Naik, 2007, Biochemistry.

Sulfur transfer from IscS to IscU: the first step in iron-sulfur cluster biosynthesis.

J. Agar, I. Amster, J. Frazzon, 2001, Journal of the American Chemical Society.

Assembly of Iron-Sulfur Clusters

D. Dean, D. Flint, V. Cash, 1998, The Journal of Biological Chemistry.

Formation and properties of [4Fe-4S] clusters on the IscU scaffold protein.

D. Dean, M. Unciuleac, S. Naik, 2007, Biochemistry.

Purification and Biophysical Characterization of a New [2Fe-2S] Ferredoxin from Azotobacter vinelandii, a Putative [Fe-S] Cluster Assembly/Repair Protein*

B. Burgess, D. Dean, Y. Jung, 1999, The Journal of Biological Chemistry.

Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis.

Robert H. White, R. White, D. Dean, 1993, Proceedings of the National Academy of Sciences of the United States of America.

Biochemical and genetic analysis of the nifUSVWZM cluster from Azotobacter vinelandii

M. Weiss, W. Newton, D. Dean, 1989, Molecular and General Genetics MGG.

Nitrogenase metalloclusters: structures, organization, and synthesis

J. Bolin, D. Dean, L. Zheng, 1993, Journal of bacteriology.

Controlled Expression of nif and isc Iron-Sulfur Protein Maturation Components Reveals Target Specificity and Limited Functional Replacement between the Two Systems

D. Dean, Deborah C. Johnson, M. Unciuleac, 2007, Journal of bacteriology.

NifS-mediated assembly of [4Fe-4S] clusters in the N- and C-terminal domains of the NifU scaffold protein.

C. Krebs, J. Agar, J. Frazzon, 2005, Biochemistry.

Escherichia coli ribosomal protein S8 feedback regulates part of spc operon

M. Nomura, J. Yates, D. Dean, 1981, Nature.

Characterization of the γ Protein and Its Involvement in the Metallocluster Assembly and Maturation of Dinitrogenase from Azotobacter vinelandii(*)

G. Roberts, D. Dean, M. Homer, 1995, The Journal of Biological Chemistry.

E. coli ribosomal protein L10 inhibits translation of L10 and L7/L12 mRNAs by acting at a single site

M. Nomura, J. Yates, D. Dean, 1981, Nature.

A substrate channel in the nitrogenase MoFe protein

Dennis R. Dean, Lance C. Seefeldt, L. Seefeldt, 2009, JBIC Journal of Biological Inorganic Chemistry.

Functional analysis of Arabidopsis genes involved in mitochondrial iron–sulfur cluster assembly

J. Balk, B. Winkel, U. Warek, 2007, Plant Molecular Biology.

Identification of ribosomal protein S7 as a repressor of translation within the str operon of E. coli

M. Nomura, J. Yates, D. Dean, 1981, Cell.

Feedback regulation of ribosomal protein gene expression in Escherichia coli.

M. Nomura, D. Dean, 1980, Proceedings of the National Academy of Sciences of the United States of America.

Biosynthesis of the nitrogenase active-site cofactor precursor NifB-co in Saccharomyces cerevisiae

Christopher A. Voigt, C. Voigt, D. B. Gordon, 2019, Proceedings of the National Academy of Sciences.

A Model for the Coordinate Regulation of Ribosomal Protein Synthesis

M. Nomura, D. Dean, 1983 .

Feedback regulation of ribosomal protein synthesis in Escherichia coli

M. Nomura, J. Yates, D. Dean, 1982 .

Genome Sequence of Azotobacter vinelandii, an Obligate Aerobe Specialized To Support Diverse Anaerobic Metabolic Processes

Jian Sun, Erik Wallin, Huijun Zhu, 2009, Journal of bacteriology.

The genome sequence of Azotobacter vinelandii , an obligate 1 aerobe specialized to support diverse anaerobic metabolic 2 processes 3 4 running title : Genome sequence of Azotobacter vinelandii 5 6

Balasubramanian, S. L. Stricklin, B. Goldman, 2009 .

The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene.

D. Bedwell, M. Nomura, D. Cerretti, 1983, Nucleic acids research.

Genetic and Physical Characterisation of nif and ntr Genes in Azotobacter chroococcum and A. vinelandii

J. Ramos, J. Postgate, D. Dean, 1985 .

Bioinorganic chemistry: electrons in Fe-S protein assembly.

D. Dean, P. D. Dos Santos, 2010, Nature chemical biology.

A High Frequency of Bacillus subtilis Glutamine Auxotrophs Revert to Cold Sensitivity

A. Aronson, D. Dean, D. Lamb, 1982 .

Reduction of Substrates by Nitrogenases.

L. Seefeldt, B. Hoffman, D. Dean, 2020, Chemical reviews.

Electron transfer precedes ATP hydrolysis during nitrogenase catalysis

L. Seefeldt, E. Antony, B. Hoffman, 2013, Proceedings of the National Academy of Sciences.

Overview of physiological, biochemical, and regulatory aspects of nitrogen fixation in Azotobacter vinelandii

J. W. Peters, R. Dixon, O. Einsle, 2022, Critical reviews in biochemistry and molecular biology.

Electron transfer within nitrogenase: evidence for a deficit-spending mechanism.

L. Seefeldt, B. Hoffman, Karamatullah Danyal, 2011, Biochemistry.

Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I: [Fe-S] cluster-driven protein rearrangement

P. Stephens, G. Jensen, C. Stout, 1989 .

Molecular Target Identification of Antimalarial Drugs Using Proteomic and Metabolomic Approaches

M. Cassera, A. Neilson, D. Dean, 2014 .

Mechanistic features and structure of the nitrogenase alpha-Gln195 MoFe protein.

B. J. Lemon, J. W. Peters, B. Lemon, 2001, Biochemistry.

Nitrogenase iron-molybdenum cofactor binding site: Protein conformational changes associated with cofactor binding

D. Rees, J. Howard, J. Magnuson, 1997 .

Fe protein-independent substrate reduction by nitrogenase MoFe protein variants.

J. W. Peters, L. Seefeldt, O. A. Zadvornyy, 2015, Biochemistry.

Mechanism of Nitrogenase H2 Formation by Metal-Hydride Protonation Probed by Mediated Electrocatalysis and H/D Isotope Effects.

Ross D. Milton, L. Seefeldt, S. Minteer, 2017, Journal of the American Chemical Society.

Reduction of short chain alkynes by a nitrogenase α-70Ala-substituted MoFe protein

D. Dean, W. Niehaus, S. Mayer, 2002 .

Nucleotide-iron-sulfur cluster signal transduction in the nitrogenase iron-protein: the role of Asp125.

J. Howard, D. Wolle, D. Dean, 1992, Science.

Comment on “Structural evidence for a dynamic metallocofactor during N2 reduction by Mo-nitrogenase”

Patrick L. Holland, L. Seefeldt, B. Hoffman, 2021, Science.

The nifU, nifS and nifV gene products are required for activity of all three nitrogenases of Azotobacter vinelandii

D. Dean, C. Kennedy, 1992, Molecular and General Genetics MGG.

Co‐ordination and fine‐tuning of nitrogen fixation in Azotobacter vinelandii

D. Dean, P. D. Dos Santos, 2011, Molecular microbiology.

CO2 Reduction Catalyzed by Nitrogenase: Pathways to Formate, Carbon Monoxide, and Methane.

L. Seefeldt, B. Hoffman, D. Dean, 2016, Inorganic chemistry.

The Fe Protein Cycle Associated with Nitrogenase Catalysis Requires the Hydrolysis of Two ATP for Each Single Electron Transfer Event.

L. Seefeldt, B. Hoffman, A. Badalyan, 2023, Journal of the American Chemical Society.

Competitive Substrate and Inhibitor Interactions at the Physiologically Relevant Active Site of Nitrogenase*

L. Seefeldt, D. Dean, J. Christiansen, 2000, The Journal of Biological Chemistry.

Formation and Insertion of the Nitrogenase Iron-Molybdenum Cofactor

Yilin Hu, M. Ribbe, D. Dean, 2004 .

Fe protein-independent substrate reduction by nitrogenase MoFe protein variants.

J. W. Peters, L. Seefeldt, Karamatullah Danyal, 2015, Biochemistry.

Reductive Elimination of H2 Activates Nitrogenase to Reduce the N≡N Triple Bond: Characterization of the E4(4H) Janus Intermediate in Wild-Type Enzyme.

L. Seefeldt, B. Hoffman, D. Dean, 2016, Journal of the American Chemical Society.

Catalytic Mechanism of Sep-tRNA:Cys-tRNA Synthase

D. Söll, Yuchen Liu, R. Orlando, 2011, The Journal of Biological Chemistry.

Electron transfer in nitrogenase catalysis.

L. Seefeldt, B. Hoffman, D. Dean, 2012, Current opinion in chemical biology.

Genome Sequence of Azotobacter vinelandii, an Obligate Aerobe Specialized To Support Diverse Anaerobic Metabolic Processes

B. Goldman, I. Paulsen, J. Setubal, 2009, Journal of bacteriology.