Published in J Biol Chem on January 31, 2007
NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation. Mol Cell (2008) 1.92
Mechanisms of oxidative protein folding in the bacterial cell envelope. Antioxid Redox Signal (2010) 1.42
Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue. J Biol Chem (2009) 1.05
Redox regulation of protein folding in the mitochondrial intermembrane space. Biochim Biophys Acta (2008) 1.04
Assignment strategies for large proteins by magic-angle spinning NMR: the 21-kDa disulfide-bond-forming enzyme DsbA. J Mol Biol (2010) 1.02
Solid-state NMR study of the charge-transfer complex between ubiquinone-8 and disulfide bond generating membrane protein DsbB. J Am Chem Soc (2011) 0.91
Dissecting the machinery that introduces disulfide bonds in Pseudomonas aeruginosa. MBio (2013) 0.90
Complementation of mitochondrial electron transport chain by manipulation of the NAD+/NADH ratio. Science (2016) 0.90
Mycobacterium tuberculosis vitamin K epoxide reductase homologue supports vitamin K-dependent carboxylation in mammalian cells. Antioxid Redox Signal (2011) 0.88
Structure of the disulfide bond generating membrane protein DsbB in the lipid bilayer. J Mol Biol (2013) 0.83
Going through the barrier: coupled disulfide exchange reactions promote efficient catalysis in quiescin sulfhydryl oxidase. J Biol Chem (2013) 0.82
Diversity of the Epsilonproteobacteria Dsb (disulfide bond) systems. Front Microbiol (2015) 0.78
A comparison of the endotoxin biosynthesis and protein oxidation pathways in the biogenesis of the outer membrane of Escherichia coli and Neisseria meningitidis. Front Cell Infect Microbiol (2012) 0.78
Snapshots of DsbA in action: detection of proteins in the process of oxidative folding. Science (2004) 2.18
Optimizing protein stability in vivo. Mol Cell (2009) 2.15
Oxidative protein folding in bacteria. Mol Microbiol (2002) 1.87
Active sites of thioredoxin reductases: why selenoproteins? Proc Natl Acad Sci U S A (2003) 1.69
Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm. Biochim Biophys Acta (2004) 1.67
Copper stress causes an in vivo requirement for the Escherichia coli disulfide isomerase DsbC. J Biol Chem (2005) 1.64
In vivo substrate specificity of periplasmic disulfide oxidoreductases. J Biol Chem (2004) 1.56
Overexpression of two different GTPases rescues a null mutation in a heat-induced rRNA methyltransferase. J Bacteriol (2002) 1.56
Genetic selection designed to stabilize proteins uncovers a chaperone called Spy. Nat Struct Mol Biol (2011) 1.52
Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding. Proc Natl Acad Sci U S A (2009) 1.46
Identification of the protein receptor binding site of botulinum neurotoxins B and G proves the double-receptor concept. Proc Natl Acad Sci U S A (2006) 1.41
Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase. Arch Biochem Biophys (2005) 1.41
Protein refolding by pH-triggered chaperone binding and release. Proc Natl Acad Sci U S A (2009) 1.35
The CXXC motif is more than a redox rheostat. J Biol Chem (2007) 1.35
Reaction of ferric cytochrome P450cam with peracids: kinetic characterization of intermediates on the reaction pathway. J Biol Chem (2005) 1.30
An engineered pathway for the formation of protein disulfide bonds. Science (2004) 1.29
Flavin redox chemistry precedes substrate chlorination during the reaction of the flavin-dependent halogenase RebH. Biochemistry (2006) 1.28
Kinetic mechanisms of the oxygenase from a two-component enzyme, p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii. J Biol Chem (2006) 1.26
Reconstitution of a disulfide isomerization system. J Biol Chem (2002) 1.22
Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis. J Biol Chem (2003) 1.22
Steady-state and transient kinetic analyses of taurine/alpha-ketoglutarate dioxygenase: effects of oxygen concentration, alternative sulfonates, and active-site variants on the FeIV-oxo intermediate. Biochemistry (2005) 1.21
The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner. Mol Microbiol (2007) 1.21
Adenosyltransferase tailors and delivers coenzyme B12. Nat Chem Biol (2008) 1.21
The mechanism of high Mr thioredoxin reductase from Drosophila melanogaster. J Biol Chem (2003) 1.14
The reductase of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii requires p-hydroxyphenylacetate for effective catalysis. Biochemistry (2005) 1.11
Comprehensive spectroscopic, steady state, and transient kinetic studies of a representative siderophore-associated flavin monooxygenase. J Biol Chem (2010) 1.10
Polymorphic variants of cytochrome P450 2B6 (CYP2B6.4-CYP2B6.9) exhibit altered rates of metabolism for bupropion and efavirenz: a charge-reversal mutation in the K139E variant (CYP2B6.8) impairs formation of a functional cytochrome p450-reductase complex. J Pharmacol Exp Ther (2011) 1.08
Chemistry of the catalytic conversion of phthalate into its cis-dihydrodiol during the reaction of oxygen with the reduced form of phthalate dioxygenase. Biochemistry (2005) 1.08
Chaperone activation by unfolding. Proc Natl Acad Sci U S A (2013) 1.07
Mechanism and regulation of the Two-component FMN-dependent monooxygenase ActVA-ActVB from Streptomyces coelicolor. J Biol Chem (2008) 1.06
Properties of the thioredoxin fold superfamily are modulated by a single amino acid residue. J Biol Chem (2009) 1.05
Kinetics of a two-component p-hydroxyphenylacetate hydroxylase explain how reduced flavin is transferred from the reductase to the oxygenase. Biochemistry (2007) 1.05
Use of 8-substituted-FAD analogues to investigate the hydroxylation mechanism of the flavoprotein 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase. Biochemistry (2004) 1.05
Disulfide bond isomerization in prokaryotes. Biochim Biophys Acta (2008) 1.04
The origami of thioredoxin-like folds. Protein Sci (2006) 1.04
DsbB catalyzes disulfide bond formation de novo. J Biol Chem (2002) 1.04
Rates of the phthalate dioxygenase reaction with oxygen are dramatically increased by interactions with phthalate and phthalate oxygenase reductase. Biochemistry (2004) 1.03
Identification of the ubiquinone-binding domain in the disulfide catalyst disulfide bond protein B. J Biol Chem (2001) 1.03
The biological activity of botulinum neurotoxin type C is dependent upon novel types of ganglioside binding sites. Mol Microbiol (2011) 1.00
Spectroscopic investigations of intermediates in the reaction of cytochrome P450(BM3)-F87G with surrogate oxygen atom donors. J Inorg Biochem (2006) 0.98
Elucidating the role of the proximal cysteine hydrogen-bonding network in ferric cytochrome P450cam and corresponding mutants using magnetic circular dichroism spectroscopy. Biochemistry (2011) 0.97
Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site. J Biol Chem (2003) 0.97
Laboratory evolution of one disulfide isomerase to resemble another. Proc Natl Acad Sci U S A (2007) 0.95
Substitutions of the "bridging" aspartate 178 result in profound changes in the reactivity of the Rieske center of phthalate dioxygenase. Biochemistry (2006) 0.94
Isolation of bacteria envelope proteins. Methods Mol Biol (2013) 0.94
Insight into disulfide bond catalysis in Chlamydia from the structure and function of DsbH, a novel oxidoreductase. J Biol Chem (2007) 0.94
Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway. J Mol Biol (2008) 0.94
Direct observation of a novel perturbed oxyferrous catalytic intermediate during reduced putidaredoxin-initiated turnover of cytochrome P-450-CAM: probing the effector role of putidaredoxin in catalysis. J Biol Chem (2005) 0.93
Disulfide bond isomerization in prokaryotes. Biochemistry (2003) 0.93
LuxG is a functioning flavin reductase for bacterial luminescence. J Bacteriol (2007) 0.93
Replacement of tyrosine residues by phenylalanine in cytochrome P450cam alters the formation of Cpd II-like species in reactions with artificial oxidants. J Biol Inorg Chem (2008) 0.93
Acid-base catalysis in the mechanism of thioredoxin reductase from Drosophila melanogaster. Biochemistry (2008) 0.92
Disulfide bond formation involves a quinhydrone-type charge-transfer complex. Proc Natl Acad Sci U S A (2003) 0.92
Rapid kinetics investigations of peracid oxidation of ferric cytochrome P450cam: nature and possible function of compound ES. J Inorg Biochem (2006) 0.91
The "bridging" aspartate 178 in phthalate dioxygenase facilitates interactions between the Rieske center and the iron(II)--mononuclear center. Biochemistry (2006) 0.91
Studies on the mechanism of p-hydroxyphenylacetate 3-hydroxylase from Pseudomonas aeruginosa: a system composed of a small flavin reductase and a large flavin-dependent oxygenase. Biochemistry (2010) 0.91
Identification of acid-base catalytic residues of high-Mr thioredoxin reductase from Plasmodium falciparum. J Biol Chem (2006) 0.89
The relationship of the redox potentials of thioredoxin and thioredoxin reductase from Drosophila melanogaster to the enzymatic mechanism: reduced thioredoxin is the reductant of glutathione in Drosophila. Biochemistry (2007) 0.89
Mechanistic studies on a novel, highly potent gold-phosphole inhibitor of human glutathione reductase. J Biol Chem (2005) 0.88
Investigations of the catalytic mechanism of thioredoxin glutathione reductase from Schistosoma mansoni. Biochemistry (2011) 0.88
The FAD cofactor of RebC shifts to an IN conformation upon flavin reduction. Biochemistry (2008) 0.88
Evidence for conformational changes within DsbD: possible role for membrane-embedded proline residues. J Bacteriol (2006) 0.88
E. coli chaperones DnaK, Hsp33 and Spy inhibit bacterial functional amyloid assembly. Prion (2011) 0.87
Mechanistic studies with N-benzyl-1-aminobenzotriazole-inactivated CYP2B1: differential effects on the metabolism of 7-ethoxy-4-(trifluoromethyl)coumarin, testosterone, and benzphetamine. Arch Biochem Biophys (2004) 0.86
Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductase. Chem Rev (2011) 0.86
Key players involved in bacterial disulfide-bond formation. Chembiochem (2004) 0.86
Increased positive electrostatic potential in p-hydroxybenzoate hydroxylase accelerates hydroxylation but slows turnover. Biochemistry (2004) 0.85
Kinetics of reversible reductive carbonylation of heme in human cystathionine β-synthase. Biochemistry (2013) 0.85
Luciferase from Vibrio campbellii is more thermostable and binds reduced FMN better than its homologues. J Biochem (2007) 0.85
High levels of expression of the iron-sulfur proteins phthalate dioxygenase and phthalate dioxygenase reductase in Escherichia coli. Protein Expr Purif (2006) 0.85
Oxygen reactions in p-hydroxybenzoate hydroxylase utilize the H-bond network during catalysis. Biochemistry (2004) 0.85
Spectroscopic studies of the oxidation of ferric CYP153A6 by peracids: Insights into P450 higher oxidation states. Arch Biochem Biophys (2009) 0.85
Engineered pathways for correct disulfide bond oxidation. Antioxid Redox Signal (2011) 0.85
Studies of an active site mutant of the selenoprotein thioredoxin reductase: the Ser-Cys-Cys-Ser motif of the insect orthologue is not sufficient to replace the Cys-Sec dyad in the mammalian enzyme. Free Radic Biol Med (2006) 0.85
In vivo detection and quantification of chemicals that enhance protein stability. Anal Biochem (2012) 0.84
Mechanistic analysis of the inactivation of cytochrome P450 2B6 by phencyclidine: effects on substrate binding, electron transfer, and uncoupling. Drug Metab Dispos (2009) 0.84
Conformational dynamics of the isoalloxazine in substrate-free p-hydroxybenzoate hydroxylase: single-molecule studies. J Am Chem Soc (2005) 0.84
Laboratory evolution of Escherichia coli thioredoxin for enhanced catalysis of protein oxidation in the periplasm reveals a phylogenetically conserved substrate specificity determinant. J Biol Chem (2007) 0.83
Properties of p-hydroxybenzoate hydroxylase when stabilized in its open conformation. Biochemistry (2005) 0.83
The crystal structure of TrxA(CACA): Insights into the formation of a [2Fe-2S] iron-sulfur cluster in an Escherichia coli thioredoxin mutant. Protein Sci (2005) 0.83
Pre-steady-state kinetic analysis of enzyme-monitored turnover during cystathionine β-synthase-catalyzed H(2)S generation. Biochemistry (2010) 0.83
Role of Arg100 in the active site of adenosylcobalamin-dependent glutamate mutase. Biochemistry (2004) 0.82
Gamma-glutamyl hydrolase: kinetic characterization of isopeptide hydrolysis using fluorogenic substrates. Biochemistry (2008) 0.82
Pre-steady-state kinetic studies on the Glu171Gln active site mutant of adenosylcobalamin-dependent glutamate mutase. Biochemistry (2002) 0.82
Similar enzymes, different structures: phthalate dioxygenase is an alpha3alpha3 stacked hexamer, not an alpha3beta3 trimer like "normal" Rieske oxygenases. Arch Biochem Biophys (2007) 0.82
Studies of the mechanism of phenol hydroxylase: effect of mutation of proline 364 to serine. Biochemistry (2002) 0.82
The dance of disulfide formation. Nat Struct Mol Biol (2004) 0.82
The transfer of reduced flavin mononucleotide from LuxG oxidoreductase to luciferase occurs via free diffusion. Biochemistry (2013) 0.81
Role of protein flexibility in the catalytic cycle of p-hydroxybenzoate hydroxylase elucidated by the Pro293Ser mutant. Biochemistry (2002) 0.81
Broad substrate specificity of the amide synthase in S. hygroscopicus--new 20-membered macrolactones derived from geldanamycin. J Am Chem Soc (2012) 0.81
Aspartate 120 of Escherichia coli methylenetetrahydrofolate reductase: evidence for major roles in folate binding and catalysis and a minor role in flavin reactivity. Biochemistry (2005) 0.80
Chaperone discovery. Bioessays (2012) 0.80
Mutational analysis of the disulfide catalysts DsbA and DsbB. J Bacteriol (2005) 0.79
A tripartite fusion system for the selection of protein variants with increased stability in vivo. Methods Mol Biol (2013) 0.79
Functional role for the conformationally mobile phenylalanine 223 in the reaction of methylenetetrahydrofolate reductase from Escherichia coli. Biochemistry (2009) 0.78
Conformational changes combined with charge-transfer interactions are essential for reduction in catalysis by p-hydroxybenzoate hydroxylase. Biochemistry (2003) 0.78
Peroxidase-like activity of uncoupled cytochrome P450: studies with bilirubin and toxicological implications of uncoupling. Biochem Pharmacol (2012) 0.78
Function of Glu-469' in the acid-base catalysis of thioredoxin reductase from Drosophila melanogaster. Biochemistry (2008) 0.78