Non-natural olefin cyclopropanation catalyzed by diverse cytochrome P450s and other hemoproteins.

ABSTRACT: Recent work has shown that engineered variants of cytochrome P450BM3 (CYP102A1) efficiently catalyze non-natural reactions, including carbene and nitrene transfer reactions. Given the broad substrate range of natural P450 enzymes, we set out to explore if this diversity could be leveraged to generate a broad panel of new catalysts for olefin cyclopropanation (i.e., carbene transfer). Here, we took a step towards this goal by characterizing the carbene transfer activities of four new wild-type P450s that have different native substrates. All four were active and exhibited a range of product selectivities in the model reaction: cyclopropanation of styrene by using ethyl diazoacetate (EDA). Previous work on P450BM3 demonstrated that mutation of the axial coordinating cysteine, universally con

SUBMITTER: Heel T 

PROVIDER: S-EPMC4287214 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature