Sulfur oxygenase/reductase

In enzymology, a sulfur oxygenase/reductase (EC 1.13.11.55) is an enzyme that catalyzes the chemical reaction

4 sulfur + 4 H2O + O2 2 hydrogen sulfide + 2 bisulfite + 2 H+
Sulfur oxygenase/reductase
Sulfur oxygenase reductase homo24mer, Acidianus ambivalens
Identifiers
EC number1.13.11.55
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

The 3 substrates of this enzyme are sulfur, H2O, and O2, whereas its 3 products are hydrogen sulfide, bisulfite, and H+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is sulfur:oxygen oxidoreductase (hydrogen-sulfide- and sulfite-forming). Other names in common use include SOR, sulfur oxygenase, and sulfur oxygenase reductase.

References

    • Kletzin A (1989). "Coupled enzymatic production of sulfite, thiosulfate, and hydrogen sulfide from sulfur: purification and properties of a sulfur oxygenase reductase from the facultatively anaerobic archaebacterium Desulfurolobus ambivalens". J. Bacteriol. 171 (3): 1638–43. PMC 209792. PMID 2493451.
    • Kletzin A (1992). "Molecular characterization of the sor gene, which encodes the sulfur oxygenase/reductase of the thermoacidophilic Archaeum Desulfurolobus ambivalens". J. Bacteriol. 174 (18): 5854–9. PMC 207119. PMID 1522063.
    • Sun CW, Chen ZW, He ZG, Zhou PJ, Liu SJ (2003). "Purification and properties of the sulfur oxygenase/reductase from the acidothermophilic archaeon, Acidianus strain S5". Extremophiles. 7 (2): 131–4. doi:10.1007/s00792-002-0304-5. PMID 12664265.
    • Urich T, Bandeiras T, Leal S, Rachel R, Albrecht T, Zimmermann P, Scholz C, Teixeira M, Gomes CM, Kletzin A (2004). "The sulphur oxygenase reductase from Acidianus ambivalens is a multimeric protein containing a low-potential mononuclear non-haem iron centre". Biochem. J. 381 (Pt 1): 137–46. doi:10.1042/BJ20040003. PMC 1133771. PMID 15030315.


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