Ontology highlight
ABSTRACT:
SUBMITTER: McIntosh JA
PROVIDER: S-EPMC4635421 | biostudies-literature | 2015 Nov
REPOSITORIES: biostudies-literature
McIntosh John A JA Heel Thomas T Buller Andrew R AR Chio Linda L Arnold Frances H FH
Journal of the American Chemical Society 20150923 43
Almost all known members of the cytochrome P450 (CYP) superfamily conserve a key cysteine residue that coordinates the heme iron. Although mutation of this residue abolishes monooxygenase activity, recent work has shown that mutation to either serine or histidine unlocks non-natural carbene- and nitrene-transfer activities. Here we present the first crystal structure of a histidine-ligated P450. The T213A/C317H variant of the thermostable CYP119 from Sulfolobus acidocaldarius maintains heme iron ...[more]