Published September 5, 2003
| public
Journal Article
Thermostabilization of a Cytochrome P450 Peroxygenase
Abstract
Some like it hot: We previously described a laboratory‐evolved variant of the cytochrome P450 BM‐3 heme domain which functions as a peroxide‐driven hydroxylase (peroxygenase, see picture). This biocatalyst does not require additional proteins or NADPH to drive hydroxylation and is amenable to further improvements through protein engineering. Here we describe a thermostable variant whose half‐life at 57.5 °C is 50 times that of the F87A variant and 250 times that of the wildtype holoenzyme.
Additional Information
© 2003 Wiley‐VCH Verlag GmbH & Co. KGaA, Weinheim. Received: May 16, 2003. The authors thank C. A. Olson for laboratory assistance. This work was supported by the Biotechnology Research and Development Corporation (Peoria, IL), an NSF Graduate Research Fellowship awarded to P.C.C., and a Visiting Scholar Grant from the Fulbright Commission awarded to O.S. for educational exchange between the USA and Chile.Additional details
- Eprint ID
- 89084
- DOI
- 10.1002/cbic.200300660
- Resolver ID
- CaltechAUTHORS:20180823-094121427
- Biotechnology Research and Development Corporation
- NSF Graduate Research Fellowship
- Fulbright Commission
- Created
-
2018-08-23Created from EPrint's datestamp field
- Updated
-
2021-11-16Created from EPrint's last_modified field