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Identification of the Binding Site on Cytochrome P450 2B4 for Cytochrome b 5 and Cytochrome P450 Reductase*
- A. Bridges, L. Gruenke, Yan‐Tyng Chang, I. Vakser, G. Loew, L. Waskell
- Biology, ChemistryThe Journal of Biological Chemistry
- 3 July 1998
These studies indicate that the binding sites for cy tochrome b 5 and cytochrome P450 reductase are, as predicted, located on the proximal surface of cytochromes P450 2B4 and are partially overlapping but not identical.
Molecular dynamics simulations of phospholipid bilayers.
- P. Huang, J. Perez, G. Loew
- Chemistry, PhysicsJournal of biomolecular structure & dynamics
- 1 April 1994
The model and conditions used in the MD simulations led to good agreement of the calculated properties of the bilayers with available experimental results, demonstrating the reliability of the simulations.
An intermediate neglect of differential overlap technique for spectroscopy of transition-metal complexes. Ferrocene
Pharmacological profiles of fentanyl analogs at μ, δ and κ opiate receptors
Role of the heme active site and protein environment in structure, spectra, and function of the cytochrome p450s.
The hyperphagic effect of 3α-hydroxylated pregnane steroids in male rats
Calculated and experimental absolute stereochemistry of the styrene and .beta.-methylstyrene epoxides formed by cytochrome P 450cam
Cytochrome P450 cam oxidizes styrene to styrene oxide and a trace of phenylacetaldehyde; cis-β-methylstyrene to cis-β-methylstyrene oxide, cis-3-phenyl-2-propen-1-ol, and a trace of…
Evidence for central benzodiazepine receptor heterogeneity from behavior tests
Determinants of the spin state of the resting state of cytochrome P450cam
The origin of the low-spin ground state of the substrate-free ferric resting state of cytochrome P450 cam has been investigated with use of the combined techniques of restricted open-shell…
Role of Protein Environment in Horseradish Peroxidase Compound I Formation: Molecular Dynamics Simulations of Horseradish Peroxidase−HOOH Complex
Molecular dynamics simulations of the peroxide bound complex of horseradish peroxidase isoenzyme C (HRP-C−HOOH) were performed to investigate the possible role of the protein in compound I formation and propose a role of two conserved amino acids in the distal binding pocket, histidine and arginine.