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Thermostabilization of a Cytochrome P450 Peroxygenase

Salazar, Oriana and Cirino, Patrick C. and Arnold, Frances H. (2003) Thermostabilization of a Cytochrome P450 Peroxygenase. ChemBioChem, 4 (9). pp. 891-893. ISSN 1439-4227. doi:10.1002/cbic.200300660.

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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.

Item Type:Article
Related URLs:
URLURL TypeDescription DOIArticle
Cirino, Patrick C.0000-0002-7245-6205
Arnold, Frances H.0000-0002-4027-364X
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.
Funding AgencyGrant Number
Biotechnology Research and Development CorporationUNSPECIFIED
NSF Graduate Research FellowshipUNSPECIFIED
Fulbright CommissionUNSPECIFIED
Subject Keywords:cytochrome P450; directed evolution; enzymes; oxidation; peroxygenases; thermostability
Issue or Number:9
Record Number:CaltechAUTHORS:20180823-094121427
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Official Citation:Salazar, O. , Cirino, P. C. and Arnold, F. H. (2003), Thermostabilization of a Cytochrome P450 Peroxygenase. ChemBioChem, 4: 891-893. doi:10.1002/cbic.200300660
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:89084
Deposited By: Tony Diaz
Deposited On:23 Aug 2018 16:51
Last Modified:16 Nov 2021 00:32

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