Ontology highlight
ABSTRACT:
SUBMITTER: Seiffert GB
PROVIDER: S-EPMC1805521 | biostudies-literature | 2007 Feb
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20070201 9
The tungsten-iron-sulfur enzyme acetylene hydratase stands out from its class because it catalyzes a nonredox reaction, the hydration of acetylene to acetaldehyde. Sequence comparisons group the protein into the dimethyl sulfoxide reductase family, and it contains a bis-molybdopterin guanine dinucleotide-ligated tungsten atom and a cubane-type [4Fe:4S] cluster. The crystal structure of acetylene hydratase at 1.26 A now shows that the tungsten center binds a water molecule that is activated by an ...[more]