Ontology highlight
ABSTRACT:
SUBMITTER: Rao G
PROVIDER: S-EPMC6380689 | biostudies-literature | 2018 May
REPOSITORIES: biostudies-literature
Rao Guodong G Tao Lizhi L Suess Daniel L M DLM Britt R David RD
Nature chemistry 20180409 5
Biosynthesis of the [FeFe] hydrogenase active site (the 'H-cluster') requires the interplay of multiple proteins and small molecules. Among them, the radical S-adenosylmethionine enzyme HydG, a tyrosine lyase, has been proposed to generate a complex that contains an Fe(CO)<sub>2</sub>(CN) moiety that is eventually incorporated into the H-cluster. Here we describe the characterization of an intermediate in the HydG reaction: a [4Fe-4S][(Cys)Fe(CO)(CN)] species, 'Complex A', in which a CO, a CN<su ...[more]