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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
21
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pubmed:dateCreated |
2002-11-4
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pubmed:abstractText |
Reduced inorganic sulfur compounds are utilized by many bacteria as electron donors to photosynthetic or respiratory electron transport chains. This metabolism is a key component of the biogeochemical sulfur cycle. The SoxAX protein is a heterodimeric c-type cytochrome involved in thiosulfate oxidation. The crystal structures of SoxAX from the photosynthetic bacterium Rhodovulum sulfidophilum have been solved at 1.75 A resolution in the oxidized state and at 1.5 A resolution in the dithionite-reduced state, providing the first structural insights into the enzymatic oxidation of thiosulfate. The SoxAX active site contains a haem with unprecedented cysteine persulfide (cysteine sulfane) coordination. This unusual post-translational modification is also seen in sulfurtransferases such as rhodanese. Intriguingly, this enzyme shares further active site characteristics with SoxAX such as an adjacent conserved arginine residue and a strongly positive electrostatic potential. These similarities have allowed us to suggest a catalytic mechanism for enzymatic thiosulfate oxidation. The atomic coordinates and experimental structure factors have been deposited in the PDB with the accession codes 1H31, 1H32 and 1H33.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-10089316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-10089488,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-10569923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-10573417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-10722656,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-10788330,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-10894738,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-10940005,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-10956045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-11017196,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-11425697,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-11443084,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-11483494,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-11513876,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-11523998,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-11567011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-11880631,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-1334573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-15299374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-2594728,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-2663079,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-4583640,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-6614472,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-7623381,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-7723011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-7939681,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-8263940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-8377180,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-8552589,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-8591033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-8702871,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-9032080,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-9049021,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-9311786,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-9537320,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-9600846,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-9692944,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-9757107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12411478-9787643
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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 |
Nov
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
21
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5599-610
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12411478-Amino Acid Sequence,
pubmed-meshheading:12411478-Bacterial Proteins,
pubmed-meshheading:12411478-Binding Sites,
pubmed-meshheading:12411478-Crystallography, X-Ray,
pubmed-meshheading:12411478-Cytochrome c Group,
pubmed-meshheading:12411478-Heme,
pubmed-meshheading:12411478-Ligands,
pubmed-meshheading:12411478-Models, Molecular,
pubmed-meshheading:12411478-Molecular Sequence Data,
pubmed-meshheading:12411478-Oxidation-Reduction,
pubmed-meshheading:12411478-Protein Conformation,
pubmed-meshheading:12411478-Protein Folding,
pubmed-meshheading:12411478-Protein Processing, Post-Translational,
pubmed-meshheading:12411478-Proteobacteria,
pubmed-meshheading:12411478-Sequence Homology, Amino Acid,
pubmed-meshheading:12411478-Thiosulfates
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pubmed:year |
2002
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pubmed:articleTitle |
Structural basis for the oxidation of thiosulfate by a sulfur cycle enzyme.
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pubmed:affiliation |
Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences and School of Chemical Sciences, University of East Anglia, Norwich NR4 7TJ, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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