R. Davydov

发表

Substrate modulation of the properties and reactivity of the oxy-ferrous and hydroperoxo-ferric intermediates of cytochrome P450cam as shown by cryoreduction-EPR/ENDOR spectroscopy.

B. Hoffman, J. Dawson, R. Perera, 2005, Journal of the American Chemical Society.

Cryoreduction EPR and 13C, 19F ENDOR study of substrate-bound substates and solvent kinetic isotope effects in the catalytic cycle of cytochrome P450cam and its T252A mutant.

B. Hoffman, J. Dawson, S. H. Kim, 2005, Dalton transactions.

{Generation of a mixed-valent Fe(III)Fe(IV) form of intermediate Q in the reaction cycle of soluble methane monooxygenase, an analog of intermediate X in ribonucleotide reductase R2 assembly}

Carsten Krebs, Stephen J. Lippard, S. Lippard, 1998 .

Product binding to the diiron(III) and mixed-valence diiron centers of methane monooxygenase hydroxylase studied by (1,2)H and (19)F ENDOR spectroscopy.

S. Lippard, B. Hoffman, S. Smoukov, 2002, Journal of the American Chemical Society.

An EPR study of the dinuclear iron site in the soluble methane monooxygenase from Methylococcus capsulatus (Bath) reduced by one electron at 77 K: the effects of component interactions and the binding of small molecules to the diiron(III) center.

S. Lippard, B. Hoffman, A. Valentine, 1999, Biochemistry.

Radiolytic Reduction of Methane Monooxygenase Dinuclear Iron Cluster at 77 K

J. Lipscomb, A. Gräslund, K. Andersson, 1997, The Journal of Biological Chemistry.

Resonance Raman and EPR investigations of the D251N oxycytochrome P450cam/putidaredoxin complex.

S. Sligar, B. Hoffman, P. Champion, 2001, Biochemistry.

Characterization and Structure of a Zn2+ and [2Fe-2S]-containing Copper Chaperone from Archaeoglobus fulgidus*

A. Rosenzweig, T. Stemmler, B. Hoffman, 2007, Journal of Biological Chemistry.

Studies on an iron(iii)-peroxo porphyrin. Iron(III)-peroxo or iron(II)-superoxo?

M. Kleimann, N. Jux, J. Harvey, 2010, Dalton transactions.

Spectroscopic Description of the E 1 State of Mo Nitrogenase Based 2 on Mo and Fe X ‐ ray Absorption and Mo ssbauer Studies

L. Seefeldt, S. DeBeer, E. Bill, 2019 .

The role of the proximal cysteine hydrogen bonding interaction in cytochrome P450 2B4 studied by cryoreduction/EPR/ENDOR spectroscopy

L. Waskell, B. Hoffman, S. Im, 2016 .

Role of the Proximal Cysteine Hydrogen Bonding Interaction in Cytochrome P450 2B4 Studied by Cryoreduction, Electron Paramagnetic Resonance, and Electron-Nuclear Double Resonance Spectroscopy.

L. Waskell, B. Hoffman, M. Shanmugam, 2016, Biochemistry.

Electron Paramagnetic Resonance and Electron-Nuclear Double Resonance Studies of the Reactions of Cryogenerated Hydroperoxoferric–Hemoprotein Intermediates

B. Hoffman, J. Dawson, M. Sono, 2014, Biochemistry.

Compound I is the reactive intermediate in the first monooxygenation step during conversion of cholesterol to pregnenolone by cytochrome P450scc: EPR/ENDOR/cryoreduction/annealing studies.

B. Hoffman, S. Usanov, N. Strushkevich, 2012, Journal of the American Chemical Society.

EPR and ENDOR characterization of the reactive intermediates in the generation of NO by cryoreduced oxy-nitric oxide synthase from Geobacillus stearothermophilus.

B. Crane, J. Sudhamsu, B. Hoffman, 2009, Journal of the American Chemical Society.

Characterization of the Microsomal Cytochrome P450 2B4 O 2 Activation Intermediates by Cryoreduction/EPR.

L. Waskell, R. Razeghifard, S. Im, 2009 .

Characterization of the microsomal cytochrome P450 2B4 O2 activation intermediates by cryoreduction and electron paramagnetic resonance.

L. Waskell, B. Hoffman, R. Razeghifard, 2008, Biochemistry.

MECHANISTIC ENZYMOLOGY OF OXYGEN ACTIVATION BY THE CYTOCHROMES P450

S. Sligar, B. Hoffman, I. Denisov, 2002, Drug metabolism reviews.

Evidence That Compound I Is the Active Species in Both the Hydroxylase and Lyase Steps by Which P450scc Converts Cholesterol to Pregnenolone: EPR/ENDOR/Cryoreduction/Annealing Studies.

B. Hoffman, D. Smil, S. Usanov, 2015, Biochemistry.

EPR and ENDOR studies of cryoreduced compounds II of peroxidases and myoglobin. Proton-coupled electron transfer and protonation status of ferryl hemes.

B. Hoffman, J. Dawson, S. H. Kim, 2008, Biochemistry.

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.

Generation of high-spin iron(I) in a protein environment using cryoreduction.

Patrick L. Holland, B. Hoffman, P. Holland, 2013, Inorganic chemistry.

Enzymatic and Cryoreduction EPR Studies of the Hydroxylation of Methylated Nω-Hydroxy-l-arginine Analogues by Nitric Oxide Synthase from Geobacillus stearothermophilus

Sarah E. Chobot, B. Crane, B. Hoffman, 2014, Biochemistry.

Kinetic isotope effects on the rate-limiting step of heme oxygenase catalysis indicate concerted proton transfer/heme hydroxylation.

M. Ikeda-Saito, H. Fujii, B. Hoffman, 2003, Journal of the American Chemical Society.

Catalytic mechanism of heme oxygenase through EPR and ENDOR of cryoreduced oxy-heme oxygenase and its Asp 140 mutants.

M. Ikeda-Saito, H. Fujii, B. Hoffman, 2002, Journal of the American Chemical Society.

EPR and ENDOR studies of Fe(II) hemoproteins reduced and oxidized at 77 K

B. Hoffman, R. Davydov, 2008, JBIC Journal of Biological Inorganic Chemistry.

Proton transfer at helium temperatures during dioxygen activation by heme monooxygenases.

T. Rajh, M. Ikeda-Saito, B. Hoffman, 2004, Journal of the American Chemical Society.

Binuclear ruthenium-manganese complexes as simple artificial models for photosystem II in green plants

Licheng Sun, H. Berglund, S. Styring, 1997 .

Probing the oxyferrous and catalytically active ferryl states of Amphitrite ornata dehaloperoxidase by cryoreduction and EPR/ENDOR spectroscopy. Detection of compound I.

B. Hoffman, Jing Du, J. Dawson, 2010, Journal of the American Chemical Society.

Spin-transfer complexes of endohedral metallofullerenes: ENDOR and NMR evidences

V. P. Bubnov, P. Manoharan, V. Lodygina, 2003 .

Distinct reaction pathways followed upon reduction of oxy-heme oxygenase and oxy-myoglobin as characterized by Mössbauer spectroscopy.

M. Ikeda-Saito, B. Hoffman, B. Huynh, 2007, Journal of the American Chemical Society.

Synthesis and Characterization of Spin-Delocalized Carboxylate-Bridged Cu(I)−Cu(II) Mixed-Valence Complexes Having Only Oxygen Donor Ligands

S. Lippard, R. Davydov, D. Lecloux, 1998 .

An Engineered Glutamate in Biosynthetic Models of Heme-Copper Oxidases Drives Complete Product Selectivity by Tuning the Hydrogen-Bonding Network.

Yi Lu, B. Hoffman, I. Petrik, 2021, Biochemistry.

EPR and ENDOR evidence for a 1-His, hydroxo-bridged mixed-valent diiron site in Desulfovibrio vulgaris rubrerythrin.

B. Hoffman, S. Smoukov, D. Kurtz, 2003, Biochemistry.

EPR study of the mixed-valent diiron sites in mouse and herpes simplex virus ribonucleotide reductases. Effect of the tyrosyl radical on structure and reactivity of the diferric center.

A. Gräslund, A. Ehrenberg, L. Thelander, 1997, Biochemistry.

Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies.

B. Hoffman, R. Davydov, 2011, Archives of biochemistry and biophysics.

Comparison of the Mechanisms of Heme Hydroxylation by Heme Oxygenases-1 and -2: Kinetic and Cryoreduction Studies.

A. Fleischhacker, S. Ragsdale, Ireena Bagai, 2016, Biochemistry.

The use of deuterated camphor as a substrate in (1)H ENDOR studies of hydroxylation by cryoreduced oxy P450cam provides new evidence of the involvement of compound I.

B. Hoffman, J. Dawson, R. Davydov, 2013, Biochemistry.

Conformational Substates of the Oxyheme Centers in α and β Subunits of Hemoglobin As Disclosed by EPR and ENDOR Studies of Cryoreduced Protein

B. Hoffman, J. Nocek, R. Davydov, 2004 .

A superoxo-ferrous state in a reduced oxy-ferrous hemoprotein and model compounds.

H. Fujii, B. Hoffman, D. Busch, 2003, Journal of the American Chemical Society.

EPR and ENDOR characterization of intermediates in the cryoreduced oxy-nitric oxide synthase heme domain with bound L-arginine or N(G)-hydroxyarginine.

B. Masters, B. Hoffman, J. Dawson, 2002, Biochemistry.

Hydroperoxy-Heme Oxygenase Generated by Cryoreduction Catalyzes the Formation of α-meso-Hydroxyheme as Detected by EPR and ENDOR

M. Ikeda-Saito, B. Hoffman, Tadashi Yoshida, 1999 .

PH-jump-induced ADP phosphorylation in mitochondria.

L. Blumenfeld, S. Kuprin, R. Davydov, 1982, Biochimica et biophysica acta.

Mixed-Valence Cu(I)-Cu(II) and Heterodimetallic Cu(I)-M(II) Bis(carboxylate-bridged) Complexes: Structural, Electrochemical, and Spectroscopic Investigations.

S. Lippard, R. Davydov, D. Lecloux, 1998, Inorganic chemistry.

Properties and function of the diiron center of ribonucleotide reductase

S. Kuprin, A. Ehrenberg, R. Davydov, 1991 .

End-On Copper(I) Superoxo and Cu(II) Peroxo and Hydroperoxo Complexes Generated by Cryoreduction/Annealing and Characterized by EPR/ENDOR Spectroscopy.

K. Karlin, B. Hoffman, R. Davydov, 2022, Journal of the American Chemical Society.

Structure and electrochemical studies of [(trispicMeen)ClFeIII OFeIII Cl(trispicMeen)](2+). Spectroscopic characterization of the mixed-valence Fe-III OFeII form. Relevance to the active site of dinuclear iron-oxo proteins

S. Styring, P. Mialane, J. Seris, 1997 .

Intramolecular electron transfer from coordinated manganese(ii) to photogenerated ruthenium(iii)

Licheng Sun, H. Berglund, S. Styring, 1997 .

Studies on the conformational changes of metalloproteins induced by electrons in water-ethylene glycol solutions at low temperatures. III. Adrenal ferredoxin.

L. Blumenfeld, R. Vilu, A. Vanin, 1975, Biochimica et biophysica acta.

Cryoreduction of methyl-coenzyme M reductase: EPR characterization of forms, MCR(ox1) and MCR (red1).

S. Ragsdale, B. Hoffman, J. Telser, 2001, Journal of the American Chemical Society.

Identification of a hemerythrin-like domain in a P1B-type transport ATPase.

A. Rosenzweig, P. Subramanian, T. Stemmler, 2010, Biochemistry.

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.

A study of melittin, motilin and galanin in reversed micellar environments, using circular dichroism spectroscopy.

A. Gräslund, U. Langel, A. Ohman, 1996, Biophysical chemistry.

The [4Fe-4S](2+) cluster in reconstituted biotin synthase binds S-adenosyl-L-methionine.

B. Hoffman, B. Huynh, Michael K. Johnson, 2002, Journal of the American Chemical Society.

Hydroxylation of camphor by reduced oxy-cytochrome P450cam: mechanistic implications of EPR and ENDOR studies of catalytic intermediates in native and mutant enzymes.

S. Sligar, B. Hoffman, S G Sligar, 2001, Journal of the American Chemical Society.

Molecular dynamics and energy transduction in chloroplasts and mitochondria

L. Blumenfeld, R. Davydov, A. Tikhonov, 1989 .

Dioxygen activation at non-heme diiron centers: oxidation of a proximal residue in the I100W variant of toluene/o-xylene monooxygenase hydroxylase.

Sun-Hee Kim, S. Lippard, B. Hoffman, 2007, Biochemistry.

Probing the Ternary Complexes of Indoleamine and Tryptophan 2,3-Dioxygenases by Cryoreduction EPR and ENDOR Spectroscopy

Sarah J. Thackray, S. Chapman, B. Hoffman, 2010, Journal of the American Chemical Society.

Spectroscopic Description of the E1 State of Mo Nitrogenase Based on Mo and Fe X-ray Absorption and Mössbauer Studies

L. Seefeldt, B. Hoffman, S. DeBeer, 2019, Inorganic chemistry.

Electron Paramagnetic Resonance Study of the Mixed-Valent Diiron Center in Escherichia coli Ribonucleotide Reductase Produced by Reduction of Radical-Free Protein R2 at 77 K

S. Kuprin, A. Ehrenberg, R. Davydov, 1994 .

Short-lived neutral FMN and FAD semiquinones are transient intermediates in cryo-reduced yeast NADPH-cytochrome P450 reductase.

B. Hoffman, R. Davydov, L. Podust, 2019, Archives of biochemistry and biophysics.

Two-Dimensional ESEEM Spectroscopy of Nitrogen Hyperfine Couplings in Methemerythrin and Azidomethemerythrin

M. Bowman, S. Dikanov, R. Davydov, 1998 .

Spectroscopic and Crystallographic Evidence for the Role of a Water-Containing H-Bond Network in Oxidase Activity of an Engineered Myoglobin

Matthew O. Ross, Yi Lu, B. Hoffman, 2015, Journal of the American Chemical Society.

Studies on the conformational changes of metalloproteins induced by electrons in water—ethylene glycol solutions at low temperatures. Cytochrome C

L. Blumenfeld, R. Davydov, N.S. Fel', 1974, FEBS letters.

Mixed-valent μ-oxo-bridged diiron complexes produced by radiolytic reduction at 77 K studied by EPR

M. Fontecave, A. Gräslund, A. Ehrenberg, 1997, JBIC Journal of Biological Inorganic Chemistry.

Effect of the tyrosyl radical on the reduction and structure of the Escherichia coli ribonucleotide reductase protein R2 diferric site as probed by EPR on the mixed-valent state.

M. Sahlin, A. Gräslund, S. Kuprin, 1996, Biochemistry.

Towards artificial photosynthesis — Light-induced intramolecular electron transfer from manganese (II) to ruthenium (III) in a binuclear complex

Licheng Sun, H. Berglund, S. Styring, 1997 .

Studies on the conformational changes of metalloproteins induced by electrons in water—ethyleneglycol solutions at low temperatures. Haemoglobin

L. Blumenfeld, R. Davydov, R.O. Vilu, 1974, FEBS letters.

Synthesis and spectroscopic studies of non-heme diiron(III) species with a terminal hydroperoxide ligand: models for hemerythrin.

K. Hodgson, S. Lippard, B. Hedman, 2001, Inorganic Chemistry.

EPR and ENDOR of catalytic intermediates in cryoreduced native and mutant oxy-cytochromes P450cam: Mutation-induced changes in the proton delivery system [15]

S. Sligar, B. Hoffman, Roman Davydov, 1999 .

Permeability of the fullerene cage of endometallofullerene for electron spin density

V. P. Bubnov, R. Davydov, V. K. Koltover, 2002 .

Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies.

B. Hoffman, R. Davydov, 2011, Archives of biochemistry and biophysics.

The nonequilibrium structures of organometallic complexes acting as the active centers of enzymes

R. Vilu, A. Vanin, L. A. Blyumenfel'd, 1974 .

Electron Paramagnetic Resonance and Electron-Nuclear Double Resonance Studies of the Reactions of Cryogenerated Hydroperoxoferric–Hemoprotein Intermediates

B. Hoffman, J. Dawson, M. Sono, 2014, Biochemistry.

EPR and ENDOR characterization of the reactive intermediates in the generation of NO by cryoreduced oxy-nitric oxide synthase from Geobacillus stearothermophilus.

B. Crane, J. Sudhamsu, B. Hoffman, 2009, Journal of the American Chemical Society.

Electron paramagnetic resonance study of the S=1/2 ground state of a radiolysis-generated manganese(III)-trimanganese(IV) form of [Mn-IV;O-4(6)(bipy)(6)](4+) (bipy=2,2'-bipyridine). Comparison with the photosynthetic Oxygen Evolving Complex

S. Styring, C. Philouze, A. Boussac, 1997 .