Putidaredoxin (PDB;1oqq) is a electron-transfer protein from Pseudomonas putida, which is homologous to ferredoxin (PDB;1a70), with [2Fe-2S] as a cofactor. This enzyme accepts one electron at a time from putidaredoxin, indicating that the two association-dissociation interactions between this enzyme and putidaredoxin occur. (A) Electron transfer from [2Fe-2S] (of putidaredoxin) to heme group of this enzyme, reducing the heme-iron from the ferric (FeIII) to the ferrous state (FeII): (A1) Indirect transfer from [2Fe-2S] to Asp38 through Cys39 (bound to [2Fe-2S]) (of putidaredoxin). (A2) Indirect transfer from Asp38 (of putidaredoxin) to Heme propionate group (acidic group) through Arg112 (of this enzyme) (see [31]). (C) Electron transfer from [2Fe-2S] (of putidaredoxin) to heme group of this enzyme, decomposing the oxygenated intermediate: The following reactions involve proton shuttle through Lys178, Arg186, Asp251, Thr252 (see [37], [41]). (B) Oxygenation of camphor by O2 at heme, giving 5-hydroxycamphor and water (H2O): (B1) Peroxygenation step from O2 to produce O-OH: (B2) Water(H2O) release from the active site: (B3) Hydroxylation step of camphor:
The 2.6-A crystal structure of Pseudomonas putida cytochrome P-450.
Crystal structure of the cytochrome P-450CAM active site mutant Thr252Ala.
Structural and electronic characterization of heme moiety in oxygenated hemoproteins by using XANES spectroscopy.
A 175-psec molecular dynamics simulation of camphor-bound cytochrome P-450cam.
Ethylbenzene hydroxylation by cytochrome P450cam.
Multichannel circular dichroism investigations of the structural stability of bacterial cytochrome P-450.
Cytochrome P450cam: crystallography, oxygen activation, and electron transfer.
Inhibitor-induced conformational change in cytochrome P-450CAM.
Substrate mobility in thiocamphor-bound cytochrome P450cam: an explanation of the conflict between the observed product profile and the X-ray structure.
Crystal structure of substrate-free Pseudomonas putida cytochrome P-450.
Effects of monovalent cations on cytochrome P-450 camphor. Evidence for preferential binding of potassium.
Crystal structure and refinement of cytochrome P450terp at 2.3 A resolution.
Comparison of the construction of a 3-D model for human thromboxane synthase using P450cam and BM-3 as templates: implications for the substrate binding pocket.
Thermodynamics of water mediating protein-ligand interactions in cytochrome P450cam: a molecular dynamics study.
Enzyme-catalyzed dehalogenation of pentachloroethane: why F87W-cytochrome P450cam is faster than wild type.
A three-dimensional model of aromatase cytochrome P450.
1H-NMR study of diamagnetic cytochrome P450cam: assignment of heme resonances and substrate dependance of one cysteinate beta proton.
Crystal structure of cytochrome P-450cam complexed with the (1S)-camphor enantiomer.
Identification of a functional water channel in cytochrome P450 enzymes.
An improved procedure for the preparation of X-ray diffraction-quality crystals of cytochrome p450cam.
P-450 binding to substrates camphor and linalool versus pressure.
Understanding the role of the essential Asp251 in cytochrome p450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect.
NMR studies of putidaredoxin: associations of putidaredoxin with NADH-putidaredoxin reductase and cytochrome p450cam.
Covalent attachment of an electroactive sulfydryl reagent in the active site of cytochrome P450cam as revealed by the crystal structure of the modified protein.
Dynamics of protein-bound water in the heme domain of P450BM3 studied by high-pressure spectroscopy: comparison with P450cam and P450 2B4.
Optical detection of cytochrome P450 by sensitizer-linked substrates.
Assignment of heme methyl 1H-NMR resonances of high-spin and low-spin ferric complexes of cytochrome p450cam using one-dimensional and two-dimensional paramagnetic signals enhancement (PASE) magnetization transfer experiments.
X-ray crystal structure and catalytic properties of Thr252Ile mutant of cytochrome P450cam: roles of Thr252 and water in the active center.
Enantiomeric discrimination of Ru-substrates by cytochrome P450cam.
Crystal structures of metyrapone- and phenylimidazole-inhibited complexes of cytochrome P-450cam.
The catalytic pathway of cytochrome p450cam at atomic resolution.
Benign synthesis of 2-ethylhexanoic acid by cytochrome P450cam: enzymatic, crystallographic, and theoretical studies.
Structural characterization of n-butyl-isocyanide complexes of cytochromes P450nor and P450cam.
A virtual high throughput screen for high affinity cytochrome P450cam substrates. Implications for in silico prediction of drug metabolism.
Probing the open state of cytochrome P450cam with ruthenium-linker substrates.
Fluorescent probes for cytochrome p450 structural characterization and inhibitor screening.
Crystal structure of the F87W/Y96F/V247L mutant of cytochrome P-450cam with 1,3,5-trichlorobenzene bound and further protein engineering for the oxidation of pentachlorobenzene and hexachlorobenzene.
Specific and non-specific effects of potassium cations on substrate-protein interactions in cytochromes P450cam and P450lin.
Impact of incorporating the 2C5 crystal structure into comparative models of cytochrome P450 2D6.
High-resolution crystal structure of cytochrome P450cam.
Crystal structures of cyanide complexes of P450cam and the oxygenase domain of inducible nitric oxide synthase-structural models of the short-lived oxygen complexes.
Crystallographic studies on the complex behavior of nicotine binding to P450cam (CYP101).
Infrared spectroscopic and mutational studies on putidaredoxin-induced conformational changes in ferrous CO-P450cam.
Conformational states of cytochrome P450cam revealed by trapping of synthetic molecular wires.
Crystal structure of the cytochrome p450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding.
A survey of active site access channels in cytochromes P450.
Production and X-ray crystallographic analysis of fully deuterated cytochrome P450cam.
Crystallographic study on the dioxygen complex of wild-type and mutant cytochrome P450cam. Implications for the dioxygen activation mechanism.
The status of high-valent metal oxo complexes in the P450 cytochromes.
Cytochrome P450 active site plasticity: attenuation of imidazole binding in cytochrome P450(cam) by an L244A mutation.
Dynamic behavior of the active site structure in bacterial cytochrome P-450.
Structure-activity correlations in pentachlorobenzene oxidation by engineered cytochrome P450cam.
Alteration of P450 distal pocket solvent leads to impaired proton delivery and changes in heme geometry.
Evaluation of the functional role of the heme-6-propionate side chain in cytochrome P450cam.
Conformational changes of cytochromes P-450cam and P-450lin induced by high pressure.
ABSORPTION AND FLUORESCENCE SPECTROSCOPY
Crystal structure of the carbon monoxide-substrate-cytochrome P-450CAM ternary complex.
The structural basis for substrate-induced changes in redox potential and spin equilibrium in cytochrome P-450CAM.
Formation, crystal structure, and rearrangement of a cytochrome P-450cam iron-phenyl complex.
Crystal structures of cytochrome P-450CAM complexed with camphane, thiocamphor, and adamantane: factors controlling P-450 substrate hydroxylation.
Roles of negatively charged surface residues of putidaredoxin in interactions with redox partners in p450cam monooxygenase system.
Multicopy molecular dynamics simulations suggest how to reconcile crystallographic and product formation data for camphor enantiomers bound to cytochrome P-450cam.