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X-ray Structure of a self-compartmentalizing sulfur cycle metalloenzyme.

Urich, Tim and Gomes, Cláudio M. and Kletzin, Arnulf and Frazão, Carlos (2006):
X-ray Structure of a self-compartmentalizing sulfur cycle metalloenzyme.
In: Science (New York, N.Y.), pp. 996-1000, 311, (5763), ISSN 1095-9203, [Article]

Abstract

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.

Item Type: Article
Erschienen: 2006
Creators: Urich, Tim and Gomes, Cláudio M. and Kletzin, Arnulf and Frazão, Carlos
Title: X-ray Structure of a self-compartmentalizing sulfur cycle metalloenzyme.
Language: English
Abstract:

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.

Journal or Publication Title: Science (New York, N.Y.)
Volume: 311
Number: 5763
Divisions: 10 Department of Biology > Sulfur Biochemistry and Microbial Bioenergetics
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10 Department of Biology
Date Deposited: 24 May 2011 08:20
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