Gene Sequence and the 1.8 Å Crystal Structure of the Tungsten-Containing Formate Dehydrogenase from Desulfovibrio gigas

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• 作者：Raaijmakers ; Hans ; et. al.
• 关键词：tungsten ; selenium ; formate dehydrogenase ; selenocysteine ; molybdopterin ; iron-sulfur cluster
• 刊名：Structure
• 出版年：2002
• 出版时间：September, 2002
• 年：2002
• 卷：10
• 期：9
• 页码：1261-1272
• 全文大小：971 K

文摘

Desulfovibrio 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.