Journal
STRUCTURE
Volume 10, Issue 9, Pages 1261-1272Publisher
CELL PRESS
DOI: 10.1016/S0969-2126(02)00826-2
Keywords
tungsten; selenium; formate dehydrogenase; selenocysteine; molybdopterin; iron-sulfur cluster
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Desulfiovibrio gigas formate dehydrogenase is the first representative of a tungsten-containing enzyme from a mesophile that has been structurally characterized. It is a heterodimer of 110 and 24 kDa subunits. The large subunit, homologous to E. coli FDH-H and to D. desulfuricans nitrate reductase, harbors the W site and one [4Fe-4S] center. No small subunit ortholog containing three [4Fe-4S] clusters has been reported. The structural homology with E. coli FDH-H shows that the essential residues (SeCys158, His159, and Arg407) at the active site are conserved. The active site is accessible via a positively charged tunnel, while product release may be facilitated, for H+ by buried waters and protonable amino acids and for CO2 through a hydrophobic channel.
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