Published in Biochemistry on March 28, 2006
A functional proline switch in cytochrome P450cam. Structure (2008) 1.05
Putidaredoxin-to-cytochrome P450cam electron transfer: differences between the two reductive steps required for catalysis. Biochemistry (2006) 1.01
Structural and dynamic implications of an effector-induced backbone amide cis-trans isomerization in cytochrome P450cam. J Mol Biol (2009) 0.96
Cross-linking mass spectrometry and mutagenesis confirm the functional importance of surface interactions between CYP3A4 and holo/apo cytochrome b(5). Biochemistry (2012) 0.95
Solution NMR structure of putidaredoxin-cytochrome P450cam complex via a combined residual dipolar coupling-spin labeling approach suggests a role for Trp106 of putidaredoxin in complex formation. J Mol Biol (2008) 0.95
Hydrogen-deuterium exchange mass spectrometry for investigation of backbone dynamics of oxidized and reduced cytochrome P450cam. J Inorg Biochem (2007) 0.94
Specific effects of potassium ion binding on wild-type and L358P cytochrome P450cam. Biochemistry (2006) 0.91
Solution structural ensembles of substrate-free cytochrome P450(cam). Biochemistry (2012) 0.90
Redox-dependent dynamics in cytochrome P450cam. Biochemistry (2009) 0.90
Experimentally restrained molecular dynamics simulations for characterizing the open states of cytochrome P450cam. Biochemistry (2011) 0.85
Correlating structure and function of drug-metabolizing enzymes: progress and ongoing challenges. Drug Metab Dispos (2013) 0.82
Spectroscopic studies of the cytochrome P450 reaction mechanisms. Biochim Biophys Acta (2017) 0.75
MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph (1996) 39.73
Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc Natl Acad Sci U S A (1997) 13.28
Structure and chemistry of cytochrome P450. Chem Rev (2005) 5.85
The catalytic pathway of cytochrome p450cam at atomic resolution. Science (2000) 5.42
High-resolution crystal structure of cytochrome P450cam. J Mol Biol (1987) 4.63
Identification of the binding site on cytochrome P450 2B4 for cytochrome b5 and cytochrome P450 reductase. J Biol Chem (1998) 2.13
Bacterial P-450cam methylene monooxygenase components: cytochrome m, putidaredoxin, and putidaredoxin reductase. Methods Enzymol (1978) 1.90
Synthesis, bacterial expression, and mutagenesis of the gene coding for mammalian cytochrome b5. Proc Natl Acad Sci U S A (1986) 1.49
Autooxidation and hydroxylation reactions of oxygenated cytochrome P-450cam. J Biol Chem (1976) 1.44
A model for effector activity in a highly specific biological electron transfer complex: the cytochrome P450(cam)-putidaredoxin couple. Biochemistry (2003) 1.43
How do substrates enter and products exit the buried active site of cytochrome P450cam? 2. Steered molecular dynamics and adiabatic mapping of substrate pathways. J Mol Biol (2000) 1.37
Probing the open state of cytochrome P450cam with ruthenium-linker substrates. Proc Natl Acad Sci U S A (2001) 1.33
Molecular recognition in cytochrome P-450: mechanism for the control of uncoupling reactions. Biochemistry (1993) 1.32
The dimerization of Pseudomonas putida cytochrome P450cam: practical consequences and engineering of a monomeric enzyme. Protein Eng (1997) 1.24
Crystal structure of the carbon monoxide-substrate-cytochrome P-450CAM ternary complex. Biochemistry (1989) 1.21
Redox-dependent structural reorganization in putidaredoxin, a vertebrate-type [2Fe-2S] ferredoxin from Pseudomonas putida. J Mol Biol (2005) 1.19
An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas. Biochemistry (1994) 1.10
Detection of a high-barrier conformational change in the active site of cytochrome P450cam upon binding of putidaredoxin. J Am Chem Soc (2005) 1.09
A structure-based model for cytochrome P450cam-putidaredoxin interactions. Biochimie (1996) 1.04
The cytochrome P-450cam binding surface as defined by site-directed mutagenesis and electrostatic modeling. Biochemistry (1990) 1.03
Crystal structure of putidaredoxin, the [2Fe-2S] component of the P450cam monooxygenase system from Pseudomonas putida. J Mol Biol (2003) 1.02
L358P mutation on cytochrome P450cam simulates structural changes upon putidaredoxin binding: the structural changes trigger electron transfer to oxy-P450cam from electron donors. J Biol Chem (2004) 1.01
Single turnover kinetics of the reaction between oxycytochrome P-450cam and reduced putidaredoxin. J Biol Chem (1988) 1.01
Role of Arg112 of cytochrome p450cam in the electron transfer from reduced putidaredoxin. Analyses with site-directed mutants. J Biol Chem (1996) 0.99
NMR study on the structural changes of cytochrome P450cam upon the complex formation with putidaredoxin. Functional significance of the putidaredoxin-induced structural changes. J Biol Chem (2003) 0.99
A refined model for the solution structure of oxidized putidaredoxin. Biochemistry (1999) 0.89
Probing the interactions of putidaredoxin with redox partners in camphor P450 5-monooxygenase by mutagenesis of surface residues. J Biol Chem (1997) 0.89
Equilibrium and kinetic studies of the interaction of cytochrome P-450cam and putidaredoxin. J Biol Chem (1982) 0.89
Redox-dependent structural differences in putidaredoxin derived from homologous structure refinement via residual dipolar couplings. Biochemistry (2005) 0.88
Putidaredoxin competitively inhibits cytochrome b5-cytochrome P-450cam association: a proposed molecular model for a cytochrome P-450cam electron-transfer complex. Biochemistry (1989) 0.88
Inhibitor-induced conformational change in cytochrome P-450CAM. Biochemistry (1993) 0.88
Mechanism of electron transfer in heme proteins and models: the NMR approach. Chem Rev (2005) 0.84
A soluble α-synuclein construct forms a dynamic tetramer. Proc Natl Acad Sci U S A (2011) 2.15
A model for effector activity in a highly specific biological electron transfer complex: the cytochrome P450(cam)-putidaredoxin couple. Biochemistry (2003) 1.43
Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae. Nat Struct Biol (2002) 1.12
Detection of a high-barrier conformational change in the active site of cytochrome P450cam upon binding of putidaredoxin. J Am Chem Soc (2005) 1.09
A functional proline switch in cytochrome P450cam. Structure (2008) 1.05
Communication between the zinc and nickel sites in dimeric HypA: metal recognition and pH sensing. J Am Chem Soc (2010) 1.01
One protein, two enzymes revisited: a structural entropy switch interconverts the two isoforms of acireductone dioxygenase. J Mol Biol (2006) 1.00
The immediate-early ethylene response gene OsARD1 encodes an acireductone dioxygenase involved in recycling of the ethylene precursor S-adenosylmethionine. Plant J (2005) 1.00
XAS investigation of the structure and function of Ni in acireductone dioxygenase. Biochemistry (2002) 0.98
Substrate recognition by the multifunctional cytochrome P450 MycG in mycinamicin hydroxylation and epoxidation reactions. J Biol Chem (2012) 0.97
Structural and dynamic implications of an effector-induced backbone amide cis-trans isomerization in cytochrome P450cam. J Mol Biol (2009) 0.96
Expression and function of the human androgen-responsive gene ADI1 in prostate cancer. Neoplasia (2007) 0.95
Solution NMR structure of putidaredoxin-cytochrome P450cam complex via a combined residual dipolar coupling-spin labeling approach suggests a role for Trp106 of putidaredoxin in complex formation. J Mol Biol (2008) 0.95
Hydrogen-deuterium exchange mass spectrometry for investigation of backbone dynamics of oxidized and reduced cytochrome P450cam. J Inorg Biochem (2007) 0.94
Specific effects of potassium ion binding on wild-type and L358P cytochrome P450cam. Biochemistry (2006) 0.91
Redox-dependent dynamics in cytochrome P450cam. Biochemistry (2009) 0.90
Solution structural ensembles of substrate-free cytochrome P450(cam). Biochemistry (2012) 0.90
Acireductone dioxygenase 1 (ARD1) is an effector of the heterotrimeric G protein beta subunit in Arabidopsis. J Biol Chem (2011) 0.90
Rapid recycle (13)C',(15)N and (13)C,(13)C' heteronuclear and homonuclear multiple quantum coherence detection for resonance assignments in paramagnetic proteins: example of Ni(2+)-containing acireductone dioxygenase. J Am Chem Soc (2002) 0.87
Experimentally restrained molecular dynamics simulations for characterizing the open states of cytochrome P450cam. Biochemistry (2011) 0.85
Comparison of functional domains in vertebrate-type ferredoxins. Biochemistry (2002) 0.83
Analogs of 1-phosphonooxy-2,2-dihydroxy-3-oxo-5-(methylthio)pentane, an acyclic intermediate in the methionine salvage pathway: a new preparation and characterization of activity with E1 enolase/phosphatase from Klebsiella oxytoca. Bioorg Med Chem (2004) 0.83
A conserved histidine in vertebrate-type ferredoxins is critical for redox-dependent dynamics. Biochemistry (2003) 0.83
Characterization of metal binding in the active sites of acireductone dioxygenase isoforms from Klebsiella ATCC 8724. Biochemistry (2008) 0.83
Spring-loading the active site of cytochrome P450cam. Metallomics (2010) 0.80
Completing the circuit: direct-observe 13C,15N double-quantum spectroscopy permits sequential resonance assignments near a paramagnetic center in acireductone dioxygenase. J Am Chem Soc (2008) 0.79
(1)H, (13)C and (15)N chemical shift assignments of an enolase-phosphatase, E1, from Klebsiella oxytoca. J Biomol NMR (2004) 0.76
Metal-Dependent Function of a Mammalian Acireductone Dioxygenase. Biochemistry (2016) 0.75