Published in Arch Biochem Biophys on September 18, 2010
Identification of a key catalytic intermediate demonstrates that nitrogenase is activated by the reversible exchange of N₂ for H₂. J Am Chem Soc (2015) 0.93
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. J Am Chem Soc (2012) 0.86
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Unveiling the crucial intermediates in androgen production. Proc Natl Acad Sci U S A (2015) 0.83
Electron paramagnetic resonance and electron-nuclear double resonance studies of the reactions of cryogenerated hydroperoxoferric-hemoprotein intermediates. Biochemistry (2014) 0.82
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1H-ENDOR evidence for a hydrogen-bonding interaction that modulates the reactivity of a nonheme Fe(IV)═O unit. Inorg Chem (2012) 0.79
Enzymatic and cryoreduction EPR studies of the hydroxylation of methylated N(ω)-hydroxy-L-arginine analogues by nitric oxide synthase from Geobacillus stearothermophilus. Biochemistry (2014) 0.78
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. Biochemistry (2015) 0.78
Exploiting the Symmetry of the Resonator Mode to Enhance PELDOR Sensitivity. Appl Magn Reson (2014) 0.78
Spectroscopic and Crystallographic Evidence for the Role of a Water-Containing H-Bond Network in Oxidase Activity of an Engineered Myoglobin. J Am Chem Soc (2016) 0.77
Role of the Proximal Cysteine Hydrogen Bonding Interaction in Cytochrome P450 2B4 Studied by Cryoreduction, Electron Paramagnetic Resonance, and Electron-Nuclear Double Resonance Spectroscopy. Biochemistry (2016) 0.77
Comparison of the Mechanisms of Heme Hydroxylation by Heme Oxygenases-1 and -2: Kinetic and Cryoreduction Studies. Biochemistry (2015) 0.75
Organometallic Complex Formed by an Unconventional Radical S-Adenosylmethionine Enzyme. J Am Chem Soc (2016) 0.75
Exploring Electron/Proton Transfer and Conformational Changes in the Nitrogenase MoFe Protein and FeMo-cofactor Through Cryoreduction/EPR Measurements. Isr J Chem (2016) 0.75
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Probing the ternary complexes of indoleamine and tryptophan 2,3-dioxygenases by cryoreduction EPR and ENDOR spectroscopy. J Am Chem Soc (2010) 1.04
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The structure of formaldehyde-inhibited xanthine oxidase determined by 35 GHz 2H ENDOR spectroscopy. J Am Chem Soc (2010) 0.97
Hydroperoxoferric heme intermediate as a second electrophilic oxidant in cytochrome P450-catalyzed reactions. J Biol Inorg Chem (2004) 0.95
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A superoxo-ferrous state in a reduced oxy-ferrous hemoprotein and model compounds. J Am Chem Soc (2003) 0.91
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The influence of substrate on the spectral properties of oxyferrous wild-type and T252A cytochrome P450-CAM. Arch Biochem Biophys (2005) 0.89
Raman evidence for specific substrate-induced structural changes in the heme pocket of human cytochrome P450 aromatase during the three consecutive oxygen activation steps. Biochemistry (2006) 0.89
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Mechanism of Mo-dependent nitrogenase. Annu Rev Biochem (2009) 3.00
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An anchoring role for FeS clusters: chelation of the amino acid moiety of S-adenosylmethionine to the unique iron site of the [4Fe-4S] cluster of pyruvate formate-lyase activating enzyme. J Am Chem Soc (2002) 2.16
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. Inorg Chem (2007) 2.12
Electron-nuclear double resonance spectroscopic evidence that S-adenosylmethionine binds in contact with the catalytically active [4Fe-4S](+) cluster of pyruvate formate-lyase activating enzyme. J Am Chem Soc (2002) 1.99
Trapping H- bound to the nitrogenase FeMo-cofactor active site during H2 evolution: characterization by ENDOR spectroscopy. J Am Chem Soc (2005) 1.93
An organometallic intermediate during alkyne reduction by nitrogenase. J Am Chem Soc (2004) 1.89
Connecting nitrogenase intermediates with the kinetic scheme for N2 reduction by a relaxation protocol and identification of the N2 binding state. Proc Natl Acad Sci U S A (2007) 1.79
The yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation. Biochemistry (2009) 1.75
Intermediates trapped during nitrogenase reduction of N triple bond N, CH3-N=NH, and H2N-NH2. J Am Chem Soc (2005) 1.68
Electron inventory, kinetic assignment (E(n)), structure, and bonding of nitrogenase turnover intermediates with C2H2 and CO. J Am Chem Soc (2005) 1.57
ENDOR spectroscopy shows that guanine N1 binds to [4Fe-4S] cluster II of the S-adenosylmethionine-dependent enzyme MoaA: mechanistic implications. J Am Chem Soc (2009) 1.54
Purified particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and a copper-containing cluster. Proc Natl Acad Sci U S A (2003) 1.54
Characterization of the particulate methane monooxygenase metal centers in multiple redox states by X-ray absorption spectroscopy. Inorg Chem (2006) 1.50
Spectroscopic approaches to elucidating novel iron-sulfur chemistry in the "radical-Sam" protein superfamily. Inorg Chem (2005) 1.49
Catalytic mechanism of heme oxygenase through EPR and ENDOR of cryoreduced oxy-heme oxygenase and its Asp 140 mutants. J Am Chem Soc (2002) 1.48
Trapping a hydrazine reduction intermediate on the nitrogenase active site. Biochemistry (2005) 1.44
Coordination and mechanism of reversible cleavage of S-adenosylmethionine by the [4Fe-4S] center in lysine 2,3-aminomutase. J Am Chem Soc (2003) 1.42
The metal centers of particulate methane monooxygenase from Methylosinus trichosporium OB3b. Biochemistry (2008) 1.38
Localization of a substrate binding site on the FeMo-cofactor in nitrogenase: trapping propargyl alcohol with an alpha-70-substituted MoFe protein. Biochemistry (2003) 1.37
Dynamic docking and electron-transfer between cytochrome b5 and a suite of myoglobin surface-charge mutants. Introduction of a functional-docking algorithm for protein-protein complexes. J Am Chem Soc (2004) 1.37
Is Mo involved in hydride binding by the four-electron reduced (E4) intermediate of the nitrogenase MoFe protein? J Am Chem Soc (2010) 1.33
Diazene (HN=NH) is a substrate for nitrogenase: insights into the pathway of N2 reduction. Biochemistry (2007) 1.29
A methyldiazene (HN=N-CH3)-derived species bound to the nitrogenase active-site FeMo cofactor: Implications for mechanism. Proc Natl Acad Sci U S A (2006) 1.28
Formation of {[HIPTN(3)N]Mo(III)H}(-) by heterolytic cleavage of H(2) as established by EPR and ENDOR spectroscopy. Inorg Chem (2010) 1.25
Probing in vivo Mn2+ speciation and oxidative stress resistance in yeast cells with electron-nuclear double resonance spectroscopy. Proc Natl Acad Sci U S A (2010) 1.25
The copper chelator methanobactin from Methylosinus trichosporium OB3b binds copper(I). J Am Chem Soc (2005) 1.23
Substrate binding to NO-ferro-naphthalene 1,2-dioxygenase studied by high-resolution Q-band pulsed 2H-ENDOR spectroscopy. J Am Chem Soc (2003) 1.22
Dynamic docking and electron transfer between Zn-myoglobin and cytochrome b(5). J Am Chem Soc (2002) 1.22
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. J Am Chem Soc (2011) 1.20
Breaking the N2 triple bond: insights into the nitrogenase mechanism. Dalton Trans (2006) 1.20
Trapping an intermediate of dinitrogen (N2) reduction on nitrogenase. Biochemistry (2009) 1.20
ENDOR/HYSCORE studies of the common intermediate trapped during nitrogenase reduction of N2H2, CH3N2H, and N2H4 support an alternating reaction pathway for N2 reduction. J Am Chem Soc (2011) 1.19
Synthesis and structural characterization of integrally oxidized, metal-free phthalocyanine compounds: [H(2)(pc)][IBr(2)] and [H(2)(pc)](2)[IBr(2)]Br.C(10)H(7)Br. Inorg Chem (2002) 1.18
Identification of protonated oxygenic ligands of ribonucleotide reductase intermediate X. J Am Chem Soc (2009) 1.18
Experimental and theoretical EPR study of Jahn-Teller-active [HIPTN(3)N]MoL complexes (L = N(2), CO, NH(3)). J Am Chem Soc (2010) 1.17
EPR and ENDOR characterization of the reactive intermediates in the generation of NO by cryoreduced oxy-nitric oxide synthase from Geobacillus stearothermophilus. J Am Chem Soc (2009) 1.17
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. J Am Chem Soc (2005) 1.15
EPR and ENDOR characterization of intermediates in the cryoreduced oxy-nitric oxide synthase heme domain with bound L-arginine or N(G)-hydroxyarginine. Biochemistry (2002) 1.14
Kinetic isotope effects on the rate-limiting step of heme oxygenase catalysis indicate concerted proton transfer/heme hydroxylation. J Am Chem Soc (2003) 1.13
Characterization of the microsomal cytochrome P450 2B4 O2 activation intermediates by cryoreduction and electron paramagnetic resonance. Biochemistry (2008) 1.09
Crystal structure and characterization of particulate methane monooxygenase from Methylocystis species strain M. Biochemistry (2011) 1.09
Mechanistic enzymology of oxygen activation by the cytochromes P450. Drug Metab Rev (2002) 1.08
Rapid freeze-quench ENDOR study of chloroperoxidase compound I: the site of the radical. J Am Chem Soc (2006) 1.08
Conformational gating of electron transfer from the nitrogenase Fe protein to MoFe protein. J Am Chem Soc (2010) 1.06
A closer look at the spectroscopic properties of possible reaction intermediates in wild-type and mutant (E)-4-hydroxy-3-methylbut-2-enyl diphosphate reductase. Biochemistry (2012) 1.06
A Davies/Hahn multi-sequence for studies of spin relaxation in pulsed ENDOR. J Magn Reson (2006) 1.05
On reversible H2 loss upon N2 binding to FeMo-cofactor of nitrogenase. Proc Natl Acad Sci U S A (2013) 1.05
Probing the ternary complexes of indoleamine and tryptophan 2,3-dioxygenases by cryoreduction EPR and ENDOR spectroscopy. J Am Chem Soc (2010) 1.04
Conformational substates of the oxyheme centers in alpha and beta subunits of hemoglobin as disclosed by EPR and ENDOR studies of cryoreduced protein. Biochemistry (2004) 1.04
The interstitial atom of the nitrogenase FeMo-cofactor: ENDOR and ESEEM show it is not an exchangeable nitrogen. J Am Chem Soc (2003) 1.04
The [4Fe-4S](2+) cluster in reconstituted biotin synthase binds S-adenosyl-L-methionine. J Am Chem Soc (2002) 1.03
Dioxygen activation at non-heme diiron centers: oxidation of a proximal residue in the I100W variant of toluene/o-xylene monooxygenase hydroxylase. Biochemistry (2007) 1.03
Spectroscopy of Cu(II)-PcoC and the multicopper oxidase function of PcoA, two essential components of Escherichia coli pco copper resistance operon. Biochemistry (2002) 1.02
The interstitial atom of the nitrogenase FeMo-cofactor: ENDOR and ESEEM evidence that it is not a nitrogen. J Am Chem Soc (2005) 1.02
Faster interprotein electron transfer in a [myoglobin, b⁵] complex with a redesigned interface. Science (2010) 1.02
Electron transfer in nitrogenase catalysis. Curr Opin Chem Biol (2012) 1.02
Distinct reaction pathways followed upon reduction of oxy-heme oxygenase and oxy-myoglobin as characterized by Mössbauer spectroscopy. J Am Chem Soc (2007) 1.01
EPR study of substrate binding to the Mn(II) active site of the bacterial antibiotic resistance enzyme FosA: a better way to examine Mn(II). J Am Chem Soc (2002) 1.00
Myoglobin and cytochrome b5: a nuclear magnetic resonance study of a highly dynamic protein complex. Biochemistry (2002) 1.00
Evidence for oxygen binding at the active site of particulate methane monooxygenase. J Am Chem Soc (2012) 1.00
ENDOR characterization of a synthetic diiron hydrazido complex as a model for nitrogenase intermediates. J Am Chem Soc (2007) 0.99
Dynamic docking of cytochrome b5 with myoglobin and alpha-hemoglobin: heme-neutralization "squares" and the binding of electron-transfer-reactive configurations. J Am Chem Soc (2007) 0.99
Electron transfer within nitrogenase: evidence for a deficit-spending mechanism. Biochemistry (2011) 0.98
Photoinitiated singlet and triplet electron transfer across a redesigned [myoglobin, cytochrome b5] interface. J Am Chem Soc (2010) 0.98
Characterization and structure of a Zn2+ and [2Fe-2S]-containing copper chaperone from Archaeoglobus fulgidus. J Biol Chem (2007) 0.97
The structure of formaldehyde-inhibited xanthine oxidase determined by 35 GHz 2H ENDOR spectroscopy. J Am Chem Soc (2010) 0.97
Proton transfer at helium temperatures during dioxygen activation by heme monooxygenases. J Am Chem Soc (2004) 0.97
How an enzyme tames reactive intermediates: positioning of the active-site components of lysine 2,3-aminomutase during enzymatic turnover as determined by ENDOR spectroscopy. J Am Chem Soc (2006) 0.96
ENDOR studies of the ligation and structure of the non-heme iron site in ACC oxidase. J Am Chem Soc (2005) 0.95
Unification of reaction pathway and kinetic scheme for N2 reduction catalyzed by nitrogenase. Proc Natl Acad Sci U S A (2012) 0.95
Modulation of substrate binding to naphthalene 1,2-dioxygenase by rieske cluster reduction/oxidation. J Am Chem Soc (2003) 0.95
A confirmation of the quench-cryoannealing relaxation protocol for identifying reduction states of freeze-trapped nitrogenase intermediates. Inorg Chem (2014) 0.94
Uncoupling nitrogenase: catalytic reduction of hydrazine to ammonia by a MoFe protein in the absence of Fe protein-ATP. J Am Chem Soc (2010) 0.94
Paramagnetic intermediates of (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE/IspG) under steady-state and pre-steady-state conditions. J Am Chem Soc (2010) 0.94
Transformation of an [Fe(η2-N2H3)]+ species to π-delocalized [Fe2(μ-N2H2)](2+/+) complexes. Angew Chem Int Ed Engl (2011) 0.94
Hopping in the electron-transfer photocycle of the 1:1 complex of Zn-cytochrome c peroxidase with cytochrome c. J Am Chem Soc (2005) 0.93
Biochemical and spectroscopic studies of the electronic structure and reactivity of a methyl-Ni species formed on methyl-coenzyme M reductase. J Am Chem Soc (2007) 0.93
Probing the oxyferrous and catalytically active ferryl states of Amphitrite ornata dehaloperoxidase by cryoreduction and EPR/ENDOR spectroscopy. Detection of compound I. J Am Chem Soc (2010) 0.92
Dynamic docking and electron transfer between myoglobin and cytochrome b(5). J Biol Inorg Chem (2002) 0.92
EPR study of the low-spin [d(3); S =(1)/(2)], Jahn-Teller-active, dinitrogen complex of a molybdenum trisamidoamine. J Am Chem Soc (2007) 0.91
A superoxo-ferrous state in a reduced oxy-ferrous hemoprotein and model compounds. J Am Chem Soc (2003) 0.91
Kinetic-dynamic model for conformational control of an electron transfer photocycle: mixed-metal hemoglobin hybrids. J Phys Chem B (2008) 0.90
Interfacial hydration, dynamics and electron transfer: multi-scale ET modeling of the transient [myoglobin, cytochrome b5] complex. Phys Chem Chem Phys (2012) 0.90
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. Dalton Trans (2005) 0.90
Identification of a hemerythrin-like domain in a P1B-type transport ATPase. Biochemistry (2010) 0.90
EPR and ENDOR studies of cryoreduced compounds II of peroxidases and myoglobin. Proton-coupled electron transfer and protonation status of ferryl hemes. Biochemistry (2008) 0.90
Characterization of the Fe-H bond in a three-coordinate terminal hydride complex of iron(I). Angew Chem Int Ed Engl (2012) 0.89
Ring-opening metathesis polymer sphere-supported seco-porphyrazines: efficient and recyclable photooxygenation catalysts. J Org Chem (2006) 0.88
Electrostatic redesign of the [myoglobin, cytochrome b5] interface to create a well-defined docked complex with rapid interprotein electron transfer. J Am Chem Soc (2009) 0.88
Simulating suppression effects in Pulsed ENDOR, and the 'hole in the middle' of Mims and Davies ENDOR Spectra. Appl Magn Reson (2010) 0.88
Enzyme control of small-molecule coordination in FosA as revealed by 31P pulsed ENDOR and ESE-EPR. J Am Chem Soc (2005) 0.88
Characterization of a cobalt-specific P(1B)-ATPase. Biochemistry (2012) 0.87
A nonclassical dihydrogen adduct of S = ½ Fe(I). J Am Chem Soc (2011) 0.86
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. J Am Chem Soc (2012) 0.86
Porphyrazines as molecular scaffolds: flexible syntheses of novel multimetallic complexes. Inorg Chem (2006) 0.86
Distance-independent charge recombination kinetics in cytochrome c-cytochrome c peroxidase complexes: compensating changes in the electronic coupling and reorganization energies. J Phys Chem B (2013) 0.86
Electron transfer precedes ATP hydrolysis during nitrogenase catalysis. Proc Natl Acad Sci U S A (2013) 0.86
17O ENDOR detection of a solvent-derived Ni-(OH(x))-Fe bridge that is lost upon activation of the hydrogenase from Desulfovibrio gigas. J Am Chem Soc (2002) 0.85