Communication
Engineering and Analysis of a Self-Sufficient Biosynthetic Cytochrome P450 PikC Fused to the RhFRED Reductase Domain
Life Sciences Institute and Department of Medicinal Chemistry, University of Michigan.
University of California, San Francisco.
In papers with more than one author, the asterisk indicates the name of the author to whom inquiries about the paper should be addressed.
Departments of Chemistry and Microbiology & Immunology, University of Michigan.
Abstract

Cytochrome P450 enzymes mediate important oxidative processes in biological systems including regio- and stereospecific hydroxylation and epoxidation reactions. The inherent requirement of these biomolecules for separate redox partner(s) significantly limits their application in biotechnology. To address this challenge, naturally occurring and/or bioengineered self-sufficient P450 systems with covalently fused redox partners have been utilized to harness their catalytic power. In this study, we describe the first in vitro characterization of a bacterial biosynthetic cytochrome P450 PikC fused to a heterologous reductase domain RhFRED that demonstrates single-component self-sufficiency. This novel fusion system not only produces a more active and effective biocatalyst but also suggests a general design for a universal reductase to generate diverse self-sufficient fusions for functional identification or industrial applications of biosynthetic P450s.
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History
- Published In Issue October 31, 2007
- Received August 3, 2007
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