Source:http://linkedlifedata.com/resource/pubmed/id/12196163
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2002-8-28
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pubmed:abstractText |
Iron-sulphur ([Fe-S]) clusters are simple inorganic prosthetic groups that are contained in a variety of proteins having functions related to electron transfer, gene regulation, environmental sensing and substrate activation. In spite of their simple structures, biological [Fe-S] clusters are not formed spontaneously. Rather, a consortium of highly conserved proteins is required for both the formation of [Fe-S] clusters and their insertion into various protein partners. Among the [Fe-S] cluster biosynthetic proteins are included a pyridoxal phosphate-dependent enzyme (NifS) that is involved in the activation of sulphur from l-cysteine, and a molecular scaffold protein (NifU) upon which [Fe-S] cluster precursors are formed. The formation or transfer of [Fe-S] clusters appears to require an electron-transfer step. Another complexity is that molecular chaperones homologous to DnaJ and DnaK are involved in some aspect of the maturation of [Fe-S]-cluster-containing proteins. It appears that the basic biochemical features of [Fe-S] cluster formation are strongly conserved in Nature, since organisms from all three life Kingdoms contain the same consortium of homologous proteins required for [Fe-S] cluster formation that were discovered in the eubacteria.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0300-5127
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
680-5
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12196163-Amino Acid Sequence,
pubmed-meshheading:12196163-Animals,
pubmed-meshheading:12196163-Azotobacter vinelandii,
pubmed-meshheading:12196163-Bacterial Proteins,
pubmed-meshheading:12196163-Conserved Sequence,
pubmed-meshheading:12196163-Escherichia coli Proteins,
pubmed-meshheading:12196163-Evolution, Molecular,
pubmed-meshheading:12196163-Humans,
pubmed-meshheading:12196163-Iron-Sulfur Proteins,
pubmed-meshheading:12196163-Molecular Sequence Data,
pubmed-meshheading:12196163-Multigene Family,
pubmed-meshheading:12196163-Sequence Alignment,
pubmed-meshheading:12196163-Sequence Homology, Amino Acid
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pubmed:year |
2002
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pubmed:articleTitle |
Biosynthesis of iron-sulphur clusters is a complex and highly conserved process.
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pubmed:affiliation |
Department of Food Sciences, ICTA, Federal University of Rio Grande do Sul, Porto Allegre, RS, 91051-970, Brazil.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Review
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