Intramolecular C(sp(3))H amination of arylsulfonyl azides with engineered and artificial myoglobin-based catalysts.

ABSTRACT: The direct conversion of aliphatic CH bonds into CN bonds provides an attractive approach to the introduction of nitrogen-containing functionalities in organic molecules. Following the recent discovery that cytochrome P450 enzymes can catalyze the cyclization of arylsulfonyl azide compounds via an intramolecular C(sp(3))H amination reaction, we have explored here the CH amination reactivity of other hemoproteins. Various heme-containing proteins, and in particular myoglobin and horseradish peroxidase, were found to be capable of catalyzing this transformation. Based on this finding, a series of engineered and artificial myoglobin variants containing active site mutations and non-native Mn- and Co-protoporphyrin IX cofactors, respectively, were prepared to investigate the effect of these st

SUBMITTER: Bordeaux M 

PROVIDER: S-EPMC4182183 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature