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Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase.

ABSTRACT: 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 adjacent aspartate residue, enabling it to attack acetylene bound in a distinct, hydrophobic pocket. This mechanism requires a strong shift of pK(a) of the aspartate, caused by a nearby low-potential [4Fe:4S] cluster. To access this previously unrecognized W-Asp active site, the protein evolved a new substrate channel distant from where it is found in other molybdenum and tungsten enzymes.

SUBMITTER: Seiffert GB 

PROVIDER: S-EPMC1805521 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature

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Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase.

Seiffert Grazyna B GB   Ullmann G Matthias GM   Messerschmidt Albrecht A   Schink Bernhard B   Kroneck Peter M H PM   Einsle Oliver O  

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]

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