Unknown

Dataset Information

0

A [4Fe-4S]-Fe(CO)(CN)-L-cysteine intermediate is the first organometallic precursor in [FeFe] hydrogenase H-cluster bioassembly.


ABSTRACT: 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)2(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- and a cysteine (Cys) molecule bind to the unique 'dangler' Fe site of the auxiliary [5Fe-4S] cluster of HydG. The identification of this intermediate-the first organometallic precursor to the H-cluster-validates the previously hypothesized HydG reaction cycle and provides a basis for elucidating the biosynthetic origin of other moieties of the H-cluster.

SUBMITTER: Rao G 

PROVIDER: S-EPMC6380689 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

A [4Fe-4S]-Fe(CO)(CN)-L-cysteine intermediate is the first organometallic precursor in [FeFe] hydrogenase H-cluster bioassembly.

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]

Similar Datasets

| S-EPMC6800375 | biostudies-literature
| S-EPMC4772725 | biostudies-literature
| S-EPMC9019909 | biostudies-literature
| S-EPMC9649522 | biostudies-literature
| S-EPMC5855289 | biostudies-literature
| S-EPMC4514031 | biostudies-literature
| S-EPMC7286669 | biostudies-literature
| S-EPMC21691 | biostudies-literature
| S-EPMC4711877 | biostudies-other
| S-EPMC9175238 | biostudies-literature