| | |
Summary: ChemBioChem 2003, 4, 891 ± 893 DOI: 10.1002/cbic.200300660 ¹ 2003 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim 891
Thermostabilization of a Cytochrome
P450 Peroxygenase
Oriana Salazar, Patrick C. Cirino, and
Frances H. Arnold*[a]
KEYWORDS:
cytochrome P450 ¥ directed evolution ¥ enzymes ¥ oxidation ¥
peroxygenases ¥ thermostability
Cytochrome P450 BM-3 is a soluble fatty acid hydroxylase
composed of a heme domain and a reductase domain on a
single polypeptide chain.[1]
We recently described a laboratory-
evolved variant of the P450 BM-3 heme domain which functions
as an H2O2-driven hydroxylase (TMperoxygenase) and does not
require NADPH, O2, or the reductase.[2]
This variant, which we
named 21B3, allows us to carry out cytochrome P450-catalyzed
biotransformations under highly simplified reaction conditions:
only the heme domain and hydrogen peroxide are needed for
substrate (fatty acid) hydroxylation. Because its heme domain
|
