Published in J Am Chem Soc on February 07, 2007
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The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriae. J Biol Chem (2003) 1.15
Epoxidation of olefins by hydroperoxo-ferric cytochrome P450. J Am Chem Soc (2003) 1.14
Evidence for basic ferryls in cytochromes P450. J Am Chem Soc (2006) 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
Evidence for two ferryl species in chloroperoxidase compound II. J Am Chem Soc (2006) 1.11
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Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science (2004) 2.29
Substrate interactions with the nitrogenase active site. Acc Chem Res (2005) 2.27
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
Chloroplast monothiol glutaredoxins as scaffold proteins for the assembly and delivery of [2Fe-2S] clusters. EMBO J (2008) 1.81
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
Formation and properties of [4Fe-4S] clusters on the IscU scaffold protein. Biochemistry (2007) 1.76
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
Redox-dependent modulation of aconitase activity in intact mitochondria. Biochemistry (2003) 1.73
MiaB, a bifunctional radical-S-adenosylmethionine enzyme involved in the thiolation and methylation of tRNA, contains two essential [4Fe-4S] clusters. Biochemistry (2007) 1.68
Intermediates trapped during nitrogenase reduction of N triple bond N, CH3-N=NH, and H2N-NH2. J Am Chem Soc (2005) 1.68
Subcellular compartmentalization of human Nfu, an iron-sulfur cluster scaffold protein, and its ability to assemble a [4Fe-4S] cluster. Proc Natl Acad Sci U S A (2003) 1.63
Characterization of the arene-oxidizing intermediate in ToMOH as a diiron(III) species. J Am Chem Soc (2007) 1.60
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
In vitro activation of apo-aconitase using a [4Fe-4S] cluster-loaded form of the IscU [Fe-S] cluster scaffolding protein. Biochemistry (2007) 1.51
Characterization of the particulate methane monooxygenase metal centers in multiple redox states by X-ray absorption spectroscopy. Inorg Chem (2006) 1.50
Heme regulates gene expression by triggering Crm1-dependent nuclear export of Bach1. EMBO J (2004) 1.49
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
Design of metal cofactors activated by a protein-protein electron transfer system. Proc Natl Acad Sci U S A (2006) 1.47
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
Coordination of adenosylmethionine to a unique iron site of the [4Fe-4S] of pyruvate formate-lyase activating enzyme: a Mössbauer spectroscopic study. J Am Chem Soc (2002) 1.41
Characterization of the cofactor composition of Escherichia coli biotin synthase. Biochemistry (2004) 1.40
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
Characterization of MOCS1A, an oxygen-sensitive iron-sulfur protein involved in human molybdenum cofactor biosynthesis. J Biol Chem (2004) 1.36
Structure and catalytic mechanism of heme oxygenase. Nat Prod Rep (2007) 1.35
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
(Mu-1,2-peroxo)diiron(III/III) complex as a precursor to the diiron(III/IV) intermediate X in the assembly of the iron-radical cofactor of ribonucleotide reductase from mouse. Biochemistry (2007) 1.33
Dioxygen activation at non-heme diiron centers: characterization of intermediates in a mutant form of toluene/o-xylene monooxygenase hydroxylase. J Am Chem Soc (2006) 1.32
Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase function. J Biol Chem (2004) 1.31
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
A flavodiiron protein and high molecular weight rubredoxin from Moorella thermoacetica with nitric oxide reductase activity. Biochemistry (2003) 1.27
Nature of the Fe-O2 bonding in oxy-myoglobin: effect of the protein. J Am Chem Soc (2008) 1.25
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
Reversible redox-dependent modulation of mitochondrial aconitase and proteolytic activity during in vivo cardiac ischemia/reperfusion. Proc Natl Acad Sci U S A (2005) 1.24
FeNO structure in distal pocket mutants of myoglobin based on resonance Raman spectroscopy. Biochemistry (2003) 1.24
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
Characterization of a direct oxygen sensor heme protein from Escherichia coli. Effects of the heme redox states and mutations at the heme-binding site on catalysis and structure. J Biol Chem (2002) 1.22
Dynamic docking and electron transfer between Zn-myoglobin and cytochrome b(5). J Am Chem Soc (2002) 1.22
NifS-mediated assembly of [4Fe-4S] clusters in the N- and C-terminal domains of the NifU scaffold protein. Biochemistry (2005) 1.21
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
Stoichiometric production of hydrogen peroxide and parallel formation of ferric multimers through decay of the diferric-peroxo complex, the first detectable intermediate in ferritin mineralization. Biochemistry (2002) 1.18
Identification of protonated oxygenic ligands of ribonucleotide reductase intermediate X. J Am Chem Soc (2009) 1.18
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
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
Native Escherichia coli SufA, coexpressed with SufBCDSE, purifies as a [2Fe-2S] protein and acts as an Fe-S transporter to Fe-S target enzymes. J Am Chem Soc (2009) 1.16
A comparative resonance Raman analysis of heme-binding PAS domains: heme iron coordination structures of the BjFixL, AxPDEA1, EcDos, and MtDos proteins. Biochemistry (2002) 1.16
Role of the [2Fe-2S] cluster in recombinant Escherichia coli biotin synthase. Biochemistry (2004) 1.15
Heme oxygenase reveals its strategy for catalyzing three successive oxygenation reactions. Acc Chem Res (2010) 1.15
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
The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriae. J Biol Chem (2003) 1.15
A new way to degrade heme: the Mycobacterium tuberculosis enzyme MhuD catalyzes heme degradation without generating CO. J Biol Chem (2013) 1.14
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
Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies. Arch Biochem Biophys (2010) 1.10
Characterization of a peroxodiiron(III) intermediate in the T201S variant of toluene/o-xylene monooxygenase hydroxylase from Pseudomonas sp. OX1. J Am Chem Soc (2009) 1.09
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
Use of a chemical trigger for electron transfer to characterize a precursor to cluster X in assembly of the iron-radical cofactor of Escherichia coli ribonucleotide reductase. Biochemistry (2004) 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
Structural characterization of the fleeting ferric peroxo species in myoglobin: experiment and theory. J Am Chem Soc (2007) 1.06
A Davies/Hahn multi-sequence for studies of spin relaxation in pulsed ENDOR. J Magn Reson (2006) 1.05
Spectroscopic characterization of site-specific [Fe(4)S(4)] cluster chemistry in ferredoxin:thioredoxin reductase: implications for the catalytic mechanism. J Am Chem Soc (2005) 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