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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5763
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pubmed:dateCreated |
2006-2-17
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pubmed:databankReference |
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
17
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pubmed:volume |
311
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
996-1000
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:16484493-Acidianus,
pubmed-meshheading:16484493-Amino Acid Sequence,
pubmed-meshheading:16484493-Archaeal Proteins,
pubmed-meshheading:16484493-Binding Sites,
pubmed-meshheading:16484493-Catalysis,
pubmed-meshheading:16484493-Catalytic Domain,
pubmed-meshheading:16484493-Crystallization,
pubmed-meshheading:16484493-Crystallography, X-Ray,
pubmed-meshheading:16484493-Hot Temperature,
pubmed-meshheading:16484493-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:16484493-Iron,
pubmed-meshheading:16484493-Ligands,
pubmed-meshheading:16484493-Models, Molecular,
pubmed-meshheading:16484493-Molecular Sequence Data,
pubmed-meshheading:16484493-Oxidation-Reduction,
pubmed-meshheading:16484493-Oxidoreductases Acting on Sulfur Group Donors,
pubmed-meshheading:16484493-Protein Conformation,
pubmed-meshheading:16484493-Protein Folding,
pubmed-meshheading:16484493-Protein Structure, Quaternary,
pubmed-meshheading:16484493-Protein Structure, Tertiary,
pubmed-meshheading:16484493-Recombinant Proteins,
pubmed-meshheading:16484493-Static Electricity,
pubmed-meshheading:16484493-Sulfur
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pubmed:year |
2006
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pubmed:articleTitle |
X-ray Structure of a self-compartmentalizing sulfur cycle metalloenzyme.
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pubmed:affiliation |
Darmstadt University of Technology, Institute of Microbiology and Genetics, Schnittspahnstrasse 10, 64287 Darmstadt, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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