EC |
1.8.5.5 |
Accepted name: |
thiosulfate reductase (quinone) |
Reaction: |
sulfite + hydrogen sulfide + a quinone = thiosulfate + a quinol |
Other name(s): |
phsABC (gene names) |
Systematic name: |
sulfite,hydrogen sulfide:quinone oxidoreductase |
Comments: |
The enzyme, characterized from the bacterium Salmonella enterica, is similar to EC 1.17.5.3, formate dehydrogenase-N. It contains a molybdopterin-guanine dinucleotide, five [4Fe-4S] clusters and two heme b groups. The reaction occurs in vivo in the direction of thiosulfate disproportionation, which is highly endergonic. It is driven by the proton motive force that occurs across the cytoplasmic membrane. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kwan, H.S. and Barrett, E.L. Map locations and functions of Salmonella typhimurium men genes. J. Bacteriol. 159 (1984) 1090–1092. [PMID: 6384182] |
2. |
Clark, M.A. and Barrett, E.L. The phs gene and hydrogen sulfide production by Salmonella typhimurium. J. Bacteriol. 169 (1987) 2391–2397. [DOI] [PMID: 3108233] |
3. |
Alami, N. and Hallenbeck, P.C. Cloning and characterization of a gene cluster, phsBCDEF, necessary for the production of hydrogen sulfide from thiosulfate by Salmonella typhimurium. Gene 156 (1995) 53–57. [DOI] [PMID: 7737516] |
4. |
Heinzinger, N.K., Fujimoto, S.Y., Clark, M.A., Moreno, M.S. and Barrett, E.L. Sequence analysis of the phs operon in Salmonella typhimurium and the contribution of thiosulfate reduction to anaerobic energy metabolism. J. Bacteriol. 177 (1995) 2813–2820. [DOI] [PMID: 7751291] |
5. |
Stoffels, L., Krehenbrink, M., Berks, B.C. and Unden, G. Thiosulfate reduction in Salmonella enterica is driven by the proton motive force. J. Bacteriol. 194 (2012) 475–485. [DOI] [PMID: 22081391] |
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[EC 1.8.5.5 created 2016, modified 2017] |
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