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Gene sequence and the 1.8 angstrom crystal structure of the tungsten-containing formate dehydrogenase from Desulfolvibrio gigas

MPG-Autoren
http://pubman.mpdl.mpg.de/cone/persons/resource/persons78142

Huber,  R.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

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Zitation

Raaijmakers, H., Macieira, S., Dias, J. M., Teixeira, S., Bursakov, S., Huber, R., et al. (2002). Gene sequence and the 1.8 angstrom crystal structure of the tungsten-containing formate dehydrogenase from Desulfolvibrio gigas. Structure, 10(9), 1261-1272.


Zitierlink: http://hdl.handle.net/11858/00-001M-0000-0010-6E6A-2
Zusammenfassung
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.