Gene sequence and the 1.8 Å crystal structure of the tungsten-containing formate dehydrogenase from Desulfovibrio gigas

Hans Raaijmakers, Sofia Macieira, João M. Dias, Susana Teixeira, Sergey Bursakov, Robert Huber, José J. G. Moura, Isabel Moura, Maria J. Romão

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Abstract

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.

Original languageEnglish
Pages (from-to)1261-1272
Number of pages12
JournalStructure
Volume10
Issue number9
DOIs
Publication statusPublished - 1 Sep 2002

Keywords

  • Formate dehydrogenase
  • Iron-sulfur cluster
  • Molybdopterin
  • Selenium
  • Selenocysteine
  • Tungsten

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