Substrate mobility in a deeply buried active site: Analysis of norcamphor bound to cytochrome P-450cam as determined by a 201-psec molecular dynamics simulation-Reference-Cited by-同舟云学术

Substrate mobility in a deeply buried active site: Analysis of norcamphor bound to cytochrome P-450cam as determined by a 201-psec molecular dynamics simulation

Published:1992-05 Issue:1 Volume:13 Page:26-37
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Genetics
language:en
Short-container-title:Proteins

Author:

Bass Michael B.,Paulsen Mark D.,Ornstein Rick L.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Reference30 articles.

1. Deuterium isotope effects in norcamphor metabolism by cytochrome P-450cam: kinetic evidence for the two-electron reduction of a high-valent iron-oxo intermediate

2. Metabolic switching in cyctochrome P-450cam: deuterium isotope effects on regiospecificity and the monooxygenase/oxidase ratio

3. High-resolution crystal structure of cytochrome P450cam

4. The structural basis for substrate-induced changes in redox potential and spin equilibrium in cytochrome P-450CAM

5. Crystal structures of cytochrome P-450CAM complexed with camphane, thiocamphor, and adamantane: factors controlling P-450 substrate hydroxylation

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3. Specific and non-specific effects of potassium cations on substrate–protein interactions in cytochromes P450cam and P450lin;Journal of Inorganic Biochemistry;2002-09

4. Experimental and Theoretical Study of the Effect of Active-Site Constrained Substrate Motion on the Magnitude of the Observed Intramolecular Isotope Effect for the P450 101 Catalyzed Benzylic Hydroxylation of Isomeric Xylenes and 4,4‘-Dimethylbiphenyl;Journal of the American Chemical Society;1998-12-16

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