ExplorEnz: EC 1.8.5.10

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1.8.5.10

Accepted name:

[DsrC]-trisulfide reductase

Reaction:

hydrogen sulfide + a [DsrC protein]-dithiol + 2 quinone = a [DsrC protein]-trisulfide + 2 quinol

Other name(s):

DsrMKJOP complex

Systematic name:

hydrogen sulfide:[DsrC protein]-dithiol oxidoreductase (trisulfide-forming)

Comments:

This enzyme complex is present in both sulfate-reducing bacteria and sulfur-oxidizing bacteria, and acts in opposite directions during the reductive and oxidative pathways, respectively. DsrM and DsrP contain b-type hemes, DsrJ contains c-type hemes, DsrO is a ferredoxin-like protein, and DsrK is the catalytic subunit that acts as a disulfide reductase on DsrC proteins that contain a trisulfide bridge [1,3,4]. The complex receives the electrons from the membrane quinone pool [2,3].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Pott, A.S. and Dahl, C. Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur. Microbiology (Reading) 144 (1998) 1881–1894. [DOI] [PMID: 9695921]
2.	Pires, R.H., Venceslau, S.S., Morais, F., Teixeira, M., Xavier, A.V. and Pereira, I.A. Characterization of the Desulfovibrio desulfuricans ATCC 27774 DsrMKJOP complex - a membrane-bound redox complex involved in the sulfate respiratory pathway. Biochemistry 45 (2006) 249–262. [DOI] [PMID: 16388601]
3.	Grein, F., Pereira, I.A. and Dahl, C. Biochemical characterization of individual components of the Allochromatium vinosum DsrMKJOP transmembrane complex aids understanding of complex function in vivo. J. Bacteriol. 192 (2010) 6369–6377. [DOI] [PMID: 20952577]
4.	Santos, A.A., Venceslau, S.S., Grein, F., Leavitt, W.D., Dahl, C., Johnston, D.T. and Pereira, I.A. A protein trisulfide couples dissimilatory sulfate reduction to energy conservation. Science 350 (2015) 1541–1545. [DOI] [PMID: 26680199]

[EC 1.8.5.10 created 2023]