Published in J Biol Chem on April 15, 2014
Assembly-line enzymology for polyketide and nonribosomal Peptide antibiotics: logic, machinery, and mechanisms. Chem Rev (2006) 7.69
Dioxygen Activation by Enzymes Containing Binuclear Non-Heme Iron Clusters. Chem Rev (1996) 4.24
Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane. Nature (1993) 3.90
An Fe2IVO2 diamond core structure for the key intermediate Q of methane monooxygenase. Science (1997) 3.29
Crystal structures of Fe2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates. Science (2007) 3.03
The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450. J Biol Chem (1985) 2.95
The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes. J Biol Inorg Chem (2005) 2.82
Methane monooxygenase from Methylosinus trichosporium OB3b. Purification and properties of a three-component system with high specific activity from a type II methanotroph. J Biol Chem (1989) 2.80
Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science (1995) 2.68
Finding intermediates in the O2 activation pathways of non-heme iron oxygenases. Acc Chem Res (2007) 2.64
Versatility of biological non-heme Fe(II) centers in oxygen activation reactions. Nat Chem Biol (2008) 2.64
Transient intermediates of the methane monooxygenase catalytic cycle. J Biol Chem (1993) 2.24
Binding of 17O-labeled substrate and inhibitors to protocatechuate 4,5-dioxygenase-nitrosyl complex. Evidence for direct substrate binding to the active site Fe2+ of extradiol dioxygenases. J Biol Chem (1986) 1.86
Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases. J Bacteriol (2004) 1.84
Single turnover chemistry and regulation of O2 activation by the oxygenase component of naphthalene 1,2-dioxygenase. J Biol Chem (2000) 1.66
Evidence for a mu-oxo-bridged binuclear iron cluster in the hydroxylase component of methane monooxygenase. Mössbauer and EPR studies. J Biol Chem (1988) 1.65
[17O]Water and nitric oxide binding by protocatechuate 4,5-dioxygenase and catechol 2,3-dioxygenase. Evidence for binding of exogenous ligands to the active site Fe2+ of extradiol dioxygenases. J Biol Chem (1985) 1.65
Crystal structure of the hydroxylase component of methane monooxygenase from Methylosinus trichosporium OB3b. Protein Sci (1997) 1.64
Trapping and spectroscopic characterization of an FeIII-superoxo intermediate from a nonheme mononuclear iron-containing enzyme. Proc Natl Acad Sci U S A (2010) 1.57
Aromatic ring cleavage by homoprotocatechuate 2,3-dioxygenase: role of His200 in the kinetics of interconversion of reaction cycle intermediates. Biochemistry (2005) 1.57
Large kinetic isotope effects in methane oxidation catalyzed by methane monooxygenase: evidence for C-H bond cleavage in a reaction cycle intermediate. Biochemistry (1996) 1.53
Single-turnover kinetics of homoprotocatechuate 2,3-dioxygenase. Biochemistry (2004) 1.48
EPR and Mössbauer studies of protocatechuate 4,5-dioxygenase. Characterization of a new Fe2+ environment. J Biol Chem (1983) 1.47
Autooxidation and hydroxylation reactions of oxygenated cytochrome P-450cam. J Biol Chem (1976) 1.44
Homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum. A dioxygenase with catalase activity. J Biol Chem (1996) 1.43
Structure and assembly of protocatechuate 3,4-dioxygenase. Nature (1988) 1.39
Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification of sites of component interaction. J Biol Chem (1991) 1.39
Kinetics and activation thermodynamics of methane monooxygenase compound Q formation and reaction with substrates. Biochemistry (2000) 1.37
Gentisate 1,2-dioxygenase from pseudomonas. Purification, characterization, and comparison of the enzymes from Pseudomonas testosteroni and Pseudomonas acidovorans. J Biol Chem (1990) 1.25
Purification and characterization of protocatechuate 2,3-dioxygenase from Bacillus macerans: a new extradiol catecholic dioxygenase. J Bacteriol (1993) 1.22
Electron paramagnetic resonance detectable states of cytochrome P-450cam. Biochemistry (1980) 1.22
Gating effects of component B on oxygen activation by the methane monooxygenase hydroxylase component. J Biol Chem (1995) 1.22
Methane monooxygenase component B and reductase alter the regioselectivity of the hydroxylase component-catalyzed reactions. A novel role for protein-protein interactions in an oxygenase mechanism. J Biol Chem (1992) 1.22
Brevibacterium fuscum protocatechuate 3,4-dioxygenase. Purification, crystallization, and characterization. J Biol Chem (1984) 1.21
Radical intermediates in monooxygenase reactions of rieske dioxygenases. J Am Chem Soc (2007) 1.20
Biochemical and spectroscopic studies on (S)-2-hydroxypropylphosphonic acid epoxidase: a novel mononuclear non-heme iron enzyme. Biochemistry (2003) 1.20
Substrate activation for O2 reactions by oxidized metal centers in biology. Proc Natl Acad Sci U S A (2007) 1.19
Cloning, sequencing, and expression of the Pseudomonas putida protocatechuate 3,4-dioxygenase genes. J Bacteriol (1993) 1.18
Crystal structures of substrate and substrate analog complexes of protocatechuate 3,4-dioxygenase: endogenous Fe3+ ligand displacement in response to substrate binding. Biochemistry (1997) 1.18
Benzoate 1,2-dioxygenase from Pseudomonas putida: single turnover kinetics and regulation of a two-component Rieske dioxygenase. Biochemistry (2002) 1.15
Methane monooxygenase component B mutants alter the kinetics of steps throughout the catalytic cycle. Biochemistry (2001) 1.14
Visualizing the substrate-, superoxo-, alkylperoxo-, and product-bound states at the nonheme Fe(II) site of homogentisate dioxygenase. Proc Natl Acad Sci U S A (2013) 1.13
Structure of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa at 2.15 A resolution. J Mol Biol (1994) 1.13
A role of the putidaredoxin COOH-terminus in P-450cam (cytochrome m) hydroxylations. Proc Natl Acad Sci U S A (1974) 1.12
Intermediate in the O-O bond cleavage reaction of an extradiol dioxygenase. Biochemistry (2008) 1.11
Regulation of methane monooxygenase catalysis based on size exclusion and quantum tunneling. Biochemistry (2006) 1.09
A family of diiron monooxygenases catalyzing amino acid beta-hydroxylation in antibiotic biosynthesis. Proc Natl Acad Sci U S A (2010) 1.07
Oxy intermediates of homoprotocatechuate 2,3-dioxygenase: facile electron transfer between substrates. Biochemistry (2011) 1.07
Mechanistic studies of 1-aminocyclopropane-1-carboxylic acid oxidase: single turnover reaction. J Biol Inorg Chem (2004) 1.07
Thiolate ligation of the active site Fe2+ of isopenicillin N synthase derives from substrate rather than endogenous cysteine: spectroscopic studies of site-specific Cys----Ser mutated enzymes. Biochemistry (1992) 1.06
Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling. Biochemistry (1999) 1.06
The role of putidaredoxin and P450 cam in methylene hydroxylation. J Biol Chem (1972) 1.04
Mössbauer studies of cytochrome P-450 cam . Biochemistry (1973) 1.01
Cytochrome P450cam and its complexes. Mössbauer parameters of the heme iron. Biochim Biophys Acta (1976) 1.00
Substrate-mediated oxygen activation by homoprotocatechuate 2,3-dioxygenase: intermediates formed by a tyrosine 257 variant. Biochemistry (2012) 0.97
Key amino acid residues in the regulation of soluble methane monooxygenase catalysis by component B. Biochemistry (2003) 0.95
Structural basis for the role of tyrosine 257 of homoprotocatechuate 2,3-dioxygenase in substrate and oxygen activation. Biochemistry (2012) 0.94
Residues in Methylosinus trichosporium OB3b methane monooxygenase component B involved in molecular interactions with reduced- and oxidized-hydroxylase component: a role for the N-terminus. Biochemistry (2001) 0.94
Mössbauer and EPR spectroscopy of protocatechuate 3,4-dioxygenase from Pseudomonas aeruginosa. Biochim Biophys Acta (1976) 0.94
Structures of competitive inhibitor complexes of protocatechuate 3,4-dioxygenase: multiple exogenous ligand binding orientations within the active site. Biochemistry (1997) 0.93
Simultaneous binding of nitric oxide and isotopically labeled substrates or inhibitors by reduced protocatechuate 3,4-dioxygenase. J Biol Chem (1993) 0.92
17O-water and cyanide ligation by the active site iron of protocatechuate 3,4-dioxygenase. Evidence for displaceable ligands in the native enzyme and in complexes with inhibitors or transition state analogs. J Biol Chem (1984) 0.92
Intermediate P* from soluble methane monooxygenase contains a diferrous cluster. Biochemistry (2013) 0.92
Unmasking of deuterium kinetic isotope effects on the methane monooxygenase compound Q reaction by site-directed mutagenesis of component B. J Am Chem Soc (2001) 0.92
The axial tyrosinate Fe3+ ligand in protocatechuate 3,4-dioxygenase influences substrate binding and product release: evidence for new reaction cycle intermediates. Biochemistry (1998) 0.92
Protocatechuate 3,4-dioxygenase. Inhibitor studies and mechanistic implications. Biochim Biophys Acta (1977) 0.91
Transition state analogs for protocatechuate 3,4-dioxygenase. Spectroscopic and kinetic studies of the binding reactions of ketonized substrate analogs. J Biol Chem (1984) 0.86
Binding of isotopically labeled substrates, inhibitors, and cyanide by protocatechuate 3,4-dioxygenase. J Biol Chem (1989) 0.86
Structure of a dinuclear iron cluster-containing β-hydroxylase active in antibiotic biosynthesis. Biochemistry (2013) 0.85
Role of the C-terminal region of the B component of Methylosinus trichosporium OB3b methane monooxygenase in the regulation of oxygen activation. Biochemistry (2006) 0.84
A two-electron-shell game: intermediates of the extradiol-cleaving catechol dioxygenases. J Biol Inorg Chem (2014) 0.84
Effector proteins from P450(cam) and methane monooxygenase: lessons in tuning nature's powerful reagents. Biochem Biophys Res Commun (2003) 0.83
Cytochrome P450 cam: SS- dimer and -SH derivative reactivities. Biochem Biophys Res Commun (1978) 0.77