Source:http://linkedlifedata.com/resource/pubmed/id/11559031
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
2001-9-17
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pubmed:abstractText |
CH(3)CO-Thr-Glu-Ser-His-His-Lys-NH(2), a hexapeptide representing the 120-125 sequence of histone H2A, coordinates Cu(II) ions efficiently. Monomeric complexes are formed. In the major complex at physiological pH, CuH(-1)L, Cu(II) is coordinated equatorially through the imidazole nitrogen of the His-4 residue and the amide nitrogens of the Ser-3 and His-4 residues, and axially through the imidazole nitrogen of the His-5 residue. This complex reacts with H(2)O(2) and the resulting reactive oxygen intermediate efficiently oxidizes 2'-deoxyguanosine. The underlying mechanism involves the formation of Cu(III) and a metal-bound hydroxyl radical species.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Copper,
http://linkedlifedata.com/resource/pubmed/chemical/Free Radicals,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidants
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0893-228X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1177-83
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11559031-Copper,
pubmed-meshheading:11559031-Free Radicals,
pubmed-meshheading:11559031-Histones,
pubmed-meshheading:11559031-Hydrogen Peroxide,
pubmed-meshheading:11559031-Oligopeptides,
pubmed-meshheading:11559031-Oxidants,
pubmed-meshheading:11559031-Oxidation-Reduction,
pubmed-meshheading:11559031-Oxidative Stress
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pubmed:year |
2001
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pubmed:articleTitle |
Stray Cu(II) may cause oxidative damage when coordinated to the -TESHHK- sequence derived from the C-terminal tail of histone H2A.
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pubmed:affiliation |
University of Ioannina, Department of Chemistry, Ioannina 45110, Greece.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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