A method for determining two substrates binding in the same active site of cytochrome P450BM3: an explanation of high energy ω product formation
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference38 articles.
1. Binding and Oxidation of Alkyl 4-Nitrophenyl Ethers by Rabbit Cytochrome P450 1A2: Evidence for Two Binding Sites
2. Evaluation of Atypical Cytochrome P450 Kinetics with Two-Substrate Models: Evidence That Multiple Substrates Can Simultaneously Bind to Cytochrome P450 Active Sites
3. Polymorphic Variants (CYP2C9*3 and CYP2C9*5) and the F114L Active Site Mutation of CYP2C9: Effect on Atypical Kinetic Metabolism Profiles
4. Atypical Kinetic Profiles in Drug Metabolism Reactions
5. Cooperativity in Oxidations Catalyzed by Cytochrome P450 3A4
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3. Kinetics of Enzymatic Hydroxylation by Free and MNPs-Immobilized NADH-Dependent Cytochrome P450 BM3 from Bacillus megaterium;Industrial & Engineering Chemistry Research;2018-12-18
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