Protein Dynamics in Cytochrome P450 Molecular Recognition and Substrate Specificity Using 2D IR Vibrational Echo Spectroscopy
Author:
Affiliation:
1. Department of Chemistry, Stanford University, Stanford, California 94305, United States
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja109168h
Reference85 articles.
1. Flexibility of Human Cytochromes P450: Molecular Dynamics Reveals Differences between CYPs 3A4, 2C9, and 2A6, which Correlate with Their Substrate Preferences
2. Comparison of the dynamics of substrate access channels in three cytochrome P450s reveals different opening mechanisms and a novel functional role for a buried arginine
3. Multiple molecular recognition mechanisms. Cytochrome P450—A case study
4. Cytochrome P450 and Chemical Toxicology
5. Guengerich, F. P.InCytochrome P450: Structure, Mechanism, and Biochemistry;de Montellano, O., Ed.Plenum Press:New York, 2005; Vol.3, p377.
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