9e15

Structural highlights

Function

HYD1A_PYRFU Part of a bifunctional enzyme complex that functions as an NADPH-dependent hydrogen-evolving hydrogenase with sulfur-reducing activity. May play a role in hydrogen cycling during fermentative growth. Activity not exhibited with NAD. The alpha and delta subunits form the hydrogenase component that catalyzes the reduction of protons to evolve hydrogen.^{[1] [2] [3] [4] [5] [6]}

References

1. ↑ Silva PJ, de Castro B, Hagen WR. On the prosthetic groups of the NiFe sulfhydrogenase from Pyrococcus furiosus: topology, structure, and temperature-dependent redox chemistry. J Biol Inorg Chem. 1999 Jun;4(3):284-91. PMID:10439073 doi:10.1007/s007750050314
2. ↑ Silva PJ, van den Ban EC, Wassink H, Haaker H, de Castro B, Robb FT, Hagen WR. Enzymes of hydrogen metabolism in Pyrococcus furiosus. Eur J Biochem. 2000 Nov;267(22):6541-51. PMID:11054105
3. ↑ Ma K, Adams MW. Hydrogenases I and II from Pyrococcus furiosus. Methods Enzymol. 2001;331:208-16. PMID:11265463 doi:10.1016/s0076-6879(01)31059-5
4. ↑ Bryant FO, Adams MW. Characterization of hydrogenase from the hyperthermophilic archaebacterium, Pyrococcus furiosus. J Biol Chem. 1989 Mar 25;264(9):5070-9 PMID:2538471
5. ↑ Pedroni P, Della Volpe A, Galli G, Mura GM, Pratesi C, Grandi G. Characterization of the locus encoding the [Ni-Fe] sulfhydrogenase from the archaeon Pyrococcus furiosus: evidence for a relationship to bacterial sulfite reductases. Microbiology (Reading). 1995 Feb;141 ( Pt 2):449-58. PMID:7704275 doi:10.1099/13500872-141-2-449
6. ↑ Silva PJ, de Castro B, Hagen WR. On the prosthetic groups of the NiFe sulfhydrogenase from Pyrococcus furiosus: topology, structure, and temperature-dependent redox chemistry. J Biol Inorg Chem. 1999 Jun;4(3):284-91. PMID:10439073 doi:10.1007/s007750050314