Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7753829 | Journal of Inorganic Biochemistry | 2018 | 9 Pages |
Abstract
Cycloalkanes were hydroxylated by cytochrome P450Bm3 variants (CYP102A1) with decoy molecules up to 8000-fold more efficiently than the wild-type enzyme alone. Different perfluorocarboxylic acids (PFCs) optimised the product formation rate (PFR) of select variant/cycloalkane combinations but did not enhance a variant (A74G/F87V/L188Q; GVQ) containing mutations in the substrate binding pocket.192
Related Topics
Physical Sciences and Engineering
Chemistry
Inorganic Chemistry
Authors
Shaghayegh Dezvarei, Hiroki Onoda, Osami Shoji, Yoshihito Watanabe, Stephen G. Bell,