Structural highlights
Function
[SOR_ACIAM] Catalyzes the simultaneous oxidation and reduction of elemental sulfur in the presence of oxygen, with sulfite and hydrogen sulfide as products.[1]
Publication Abstract from PubMed
Numerous microorganisms oxidize sulfur for energy conservation and contribute to the global biogeochemical sulfur cycle. We have determined the 1.7 angstrom-resolution structure of the sulfur oxygenase reductase from the thermoacidophilic archaeon Acidianus ambivalens, which catalyzes an oxygen-dependent disproportionation of elemental sulfur. Twenty-four monomers form a large hollow sphere enclosing a positively charged nanocompartment. Apolar channels provide access for linear sulfur species. A cysteine persulfide and a low-potential mononuclear non-heme iron site ligated by a 2-His-1-carboxylate facial triad in a pocket of each subunit constitute the active sites, accessible from the inside of the sphere. The iron is likely the site of both sulfur oxidation and sulfur reduction.
X-ray Structure of a self-compartmentalizing sulfur cycle metalloenzyme.,Urich T, Gomes CM, Kletzin A, Frazao C Science. 2006 Feb 17;311(5763):996-1000. PMID:16484493[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Urich T, Bandeiras TM, Leal SS, Rachel R, Albrecht T, Zimmermann P, Scholz C, Teixeira M, Gomes CM, Kletzin A. The sulphur oxygenase reductase from Acidianus ambivalens is a multimeric protein containing a low-potential mononuclear non-haem iron centre. Biochem J. 2004 Jul 1;381(Pt 1):137-46. PMID:15030315 doi:http://dx.doi.org/10.1042/BJ20040003
- ↑ Urich T, Gomes CM, Kletzin A, Frazao C. X-ray Structure of a self-compartmentalizing sulfur cycle metalloenzyme. Science. 2006 Feb 17;311(5763):996-1000. PMID:16484493 doi:311/5763/996
