| Comments: |
This enzyme, which is found in thermophilic microorganisms, contains one mononuclear none-heme iron centre per subunit. Elemental sulfur is both the electron donor and one of the two known acceptors, the other being oxygen. Thiosulfate is also observed as a product, but is likely formed non-enzymically by a reaction between sulfite and sulfur [1]. This enzyme differs from EC 1.13.11.18, sulfur dioxygenase and EC 1.12.98.4, sulfhydrogenase, in that both activities occur simultaneously. |
| References: |
| 1. |
Kletzin, A. 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 (1989) 1638–1643. [DOI] [PMID: 2493451] |
| 2. |
Kletzin, A. Molecular characterization of the sor gene, which encodes the sulfur oxygenase/reductase of the thermoacidophilic Archaeum Desulfurolobus ambivalens. J. Bacteriol. 174 (1992) 5854–5859. [DOI] [PMID: 1522063] |
| 3. |
Sun, C.W., Chen, Z.W., He, Z.G., Zhou, P.J. and Liu, S.J. Purification and properties of the sulfur oxygenase/reductase from the
acidothermophilic archaeon, Acidianus strain S5. Extremophiles 7 (2003) 131–134. [DOI] [PMID: 12664265] |
| 4. |
Urich, T., Bandeiras, T.M., Leal, S.S., Rachel, R., Albrecht, T., Zimmermann, P., Scholz, C., Teixeira, M., Gomes, C.M. and Kletzin, A. The sulphur oxygenase reductase from Acidianus ambivalens is a multimeric protein containing a low-potential mononuclear non-haem iron centre. Biochem. J. 381 (2004) 137–146. [DOI] [PMID: 15030315] |
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