A substrate-binding-state mimic of H2O2-dependent cytochrome P450 produced by one-point mutagenesis and peroxygenation of non-native substrates
Author:
Affiliation:
1. Department of Chemistry
2. Graduate School of Science
3. Nagoya University
4. Nagoya 464-8602
5. Japan
6. RIKEN SPring-8 Center
7. Harima Institute
8. Sayo
9. Research Center for Materials Science
Abstract
H2O2-dependent cytochrome P450s that can catalyze monooxygenation of nonnative substrates were constructed by one-point mutagenesis.
Publisher
Royal Society of Chemistry (RSC)
Subject
Catalysis
Link
http://pubs.rsc.org/en/content/articlepdf/2016/CY/C6CY00630B
Reference52 articles.
1. Cytochrome P450: Structure, Mechanism, and Biochemistry, ed. P. R. Ortiz de Montellano, Plenum Press, New York, 2005
2. Heme-Containing Oxygenases
3. Structure and Chemistry of Cytochrome P450
4. Engineered Alkane-Hydroxylating Cytochrome P450BM3 Exhibiting Nativelike Catalytic Properties
5. Direct Conversion of Ethane to Ethanol by Engineered Cytochrome P450 BM3
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