Published in Biochemistry on August 05, 2003
Mechanism of Mo-dependent nitrogenase. Annu Rev Biochem (2009) 3.00
Ligand binding to the FeMo-cofactor: structures of CO-bound and reactivated nitrogenase. Science (2014) 1.86
Mechanism of nitrogen fixation by nitrogenase: the next stage. Chem Rev (2014) 1.83
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
Trapping an intermediate of dinitrogen (N2) reduction on nitrogenase. Biochemistry (2009) 1.20
Alkyne substrate interaction within the nitrogenase MoFe protein. J Inorg Biochem (2007) 1.18
Catalytic activities of NifEN: implications for nitrogenase evolution and mechanism. Proc Natl Acad Sci U S A (2009) 1.09
Electron transfer in nitrogenase catalysis. Curr Opin Chem Biol (2012) 1.02
A substrate channel in the nitrogenase MoFe protein. J Biol Inorg Chem (2009) 0.96
Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor. Elife (2015) 0.89
Steric control of the Hi-CO MoFe nitrogenase complex revealed by stopped-flow infrared spectroscopy. Angew Chem Int Ed Engl (2011) 0.89
EXAFS and NRVS reveal a conformational distortion of the FeMo-cofactor in the MoFe nitrogenase propargyl alcohol complex. J Inorg Biochem (2012) 0.89
Classifying the metal dependence of uncharacterized nitrogenases. Front Microbiol (2013) 0.86
Ammonia formation by a thiolate-bridged diiron amide complex as a nitrogenase mimic. Nat Chem (2013) 0.84
Azotobacter vinelandii vanadium nitrogenase: formaldehyde is a product of catalyzed HCN reduction, and excess ammonia arises directly from catalyzed azide reduction. Biochemistry (2006) 0.84
Multiple amino acid sequence alignment nitrogenase component 1: insights into phylogenetics and structure-function relationships. PLoS One (2013) 0.82
Multimetallic Cooperativity in Activation of Dinitrogen at Iron-Potassium Sites. Chem Sci (2014) 0.79
Structure and spectroscopy of a bidentate bis-homocitrate dioxo-molybdenum(VI) complex: insights relevant to the structure and properties of the FeMo-cofactor in nitrogenase. J Inorg Biochem (2012) 0.79
Uncoupling binding of substrate CO from turnover by vanadium nitrogenase. Proc Natl Acad Sci U S A (2015) 0.78
Reduction of N2 by supported tungsten clusters gives a model of the process by nitrogenase. Sci Rep (2012) 0.75
Structure, function, and formation of biological iron-sulfur clusters. Annu Rev Biochem (2005) 6.82
Mechanism of Mo-dependent nitrogenase. Annu Rev Biochem (2009) 3.00
Climbing nitrogenase: toward a mechanism of enzymatic nitrogen fixation. Acc Chem Res (2009) 2.43
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
Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistry. Curr Opin Chem Biol (2003) 1.96
Trapping H- bound to the nitrogenase FeMo-cofactor active site during H2 evolution: characterization by ENDOR spectroscopy. J Am Chem Soc (2005) 1.93
Structure of a cofactor-deficient nitrogenase MoFe protein. Science (2002) 1.91
An organometallic intermediate during alkyne reduction by nitrogenase. J Am Chem Soc (2004) 1.89
Frontiers, opportunities, and challenges in biochemical and chemical catalysis of CO2 fixation. Chem Rev (2013) 1.86
Mechanism of nitrogen fixation by nitrogenase: the next stage. Chem Rev (2014) 1.83
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 insertion of the nitrogenase iron-molybdenum cofactor. Chem Rev (2004) 1.77
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
Substrate interactions with nitrogenase: Fe versus Mo. Biochemistry (2004) 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
Nitrogen fixation: the mechanism of the Mo-dependent nitrogenase. Crit Rev Biochem Mol Biol (2003) 1.65
Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized to support diverse anaerobic metabolic processes. J Bacteriol (2009) 1.64
Nitrogenase: a draft mechanism. Acc Chem Res (2013) 1.64
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
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
Controlled expression and functional analysis of iron-sulfur cluster biosynthetic components within Azotobacter vinelandii. J Bacteriol (2006) 1.46
In vivo iron-sulfur cluster formation. Proc Natl Acad Sci U S A (2008) 1.44
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
Substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis. J Biol Chem (2004) 1.40
The metal centers of particulate methane monooxygenase from Methylosinus trichosporium OB3b. Biochemistry (2008) 1.38
(IscS-IscU)2 complex structures provide insights into Fe2S2 biogenesis and transfer. Angew Chem Int Ed Engl (2012) 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
Iron-sulfur cluster assembly: NifU-directed activation of the nitrogenase Fe protein. J Biol Chem (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
A proposed role for the Azotobacter vinelandii NfuA protein as an intermediate iron-sulfur cluster carrier. J Biol Chem (2008) 1.27
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
Determining the topology of integral membrane peptides using EPR spectroscopy. J Am Chem Soc (2006) 1.22
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
NifS-mediated assembly of [4Fe-4S] clusters in the N- and C-terminal domains of the NifU scaffold protein. Biochemistry (2005) 1.21
Molybdenum nitrogenase catalyzes the reduction and coupling of CO to form hydrocarbons. J Biol Chem (2011) 1.20
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
Localization of a catalytic intermediate bound to the FeMo-cofactor of nitrogenase. J Biol Chem (2004) 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
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