Gene sequence and the 1.8 A crystal structure of the tungsten-containing formate dehydrogenase from Desulfovibrio gigas.
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 CO(2) through a hydrophobic channel.
Raaijmakers
Hans
H
REQUIMTE/CQFB, Departamento de Química, FCT, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal.
Macieira
Sofia
S
Dias
João M
JM
Teixeira
Susana
S
Bursakov
Sergey
S
Huber
Robert
R
Moura
José J G
JJ
Moura
Isabel
I
Romão
Maria J
MJ
D000595:Amino Acid Sequence; D001665:Binding Sites; D002245:Carbon Dioxide / Q000378:metabolism; D018360:Crystallography, X-Ray; D003901:Desulfovibrio / Q000201:enzymology* / Q000235:genetics; D004583:Electrons; D005560:Formate Dehydrogenases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D011522:Protons; D017386:Sequence Homology, Amino Acid; D055672:Static Electricity; D013329:Structure-Activity Relationship; D014414:Tungsten / Q000378:metabolism*
D021122:Protein Subunits; D011522:Protons; D002245:Carbon Dioxide; D005560:Formate Dehydrogenases; D014414:Tungsten