Structural highlights
Function
HYD1B_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 beta and gamma subunits form the sulfur reducing component that catalyzes the cytoplasmic production of hydrogen sulfide in the presence of elemental sulfur. Not active in the presence of sodium sulfate, sodium sulfite, sodium thiosulfate or cysteine.[1] [2] [3] [4]
References
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ Ma K, Schicho RN, Kelly RM, Adams MW. Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: evidence for a sulfur-reducing hydrogenase ancestor. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5341-4. PMID:8389482 doi:10.1073/pnas.90.11.5341
