Redox Potential Control by Drug Binding to Cytochrome P450 3A4
Author:
Affiliation:
1. Department of Biochemistry, School of Molecular and Cellular Biology, and Beckman Institute for Advanced Science and Technology, University of Illinois, Urbana, Illinois 61801
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja074864x
Reference27 articles.
1. CYTOCHROME P-450 3A4: Regulation and Role in Drug Metabolism
2. (b) Guengerich, F. P. inCytochrome P450: Structure Mechanism, andBiochemistry, 3rd ed.; Ortiz de Montellano, P. R., Ed.; Kluwer Academic/Plenum Publishers: New York, 2005; pp 377−530.
3. Coupling of spin, substrate, and redox equilibriums in cytochrome P450
4. A thermodynamic model of regulation: modulation of redox equilibria in camphor monoxygenase.
5. Control of heme protein redox potential and reduction rate: linear free energy relation between potential and ferric spin state equilibrium
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