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ReportsX-ray Structure of a Self-Compartmentalizing Sulfur Cycle Metalloenzyme
Numerous microorganisms oxidize sulfur for energy conservation and contribute to the global biogeochemical sulfur cycle. We have determined the 1.7 angstromresolution 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.
1 Darmstadt University of Technology, Institute of Microbiology and Genetics, Schnittspahnstrasse 10, 64287 Darmstadt, Germany.
2 Universidade Nova de Lisboa, Instituto de Tecnologia Química e Biológica, Avenida da República EAN, 2781-901 Oeiras, Portugal. * To whom correspondence should be addressed. E-mail kletzin{at}bio.tu-darmstadt.de (A.K.); frazao{at}itqb.unl.pt. (C.F.)
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Science. ISSN 0036-8075 (print), 1095-9203 (online)