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rdf:type |
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lifeskim:mentions |
umls-concept:C0010760,
umls-concept:C0013850,
umls-concept:C0026336,
umls-concept:C0026339,
umls-concept:C0205099,
umls-concept:C0678594,
umls-concept:C0871161,
umls-concept:C1514562,
umls-concept:C1707455,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2827424
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pubmed:issue |
16
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pubmed:dateCreated |
1995-9-11
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pubmed:abstractText |
The electronic structure and spectrum of several models of the binuclear metal site in soluble CuA domains of cytochrome-c oxidase have been calculated by the use of an extended version of the complete neglect of differential overlap/spectroscopic method. The experimental spectra have two strong transitions of nearly equal intensity around 500 nm and a near-IR transition close to 800 nm. The model that best reproduces these features consists of a dimer of two blue (type 1) copper centers, in which each Cu atom replaces the missing imidazole on the other Cu atom. Thus, both Cu atoms have one cysteine sulfur atom and one imidazole nitrogen atom as ligands, and there are no bridging ligands but a direct Cu-Cu bond. According to the calculations, the two strong bands in the visible region originate from exciton coupling of the dipoles of the two copper monomers, and the near-IR band is a charge-transfer transition between the two Cu atoms. The known amino acid sequence has been used to construct a molecular model of the CuA site by the use of a template and energy minimization. In this model, the two ligand cysteine residues are in one turn of an alpha-helix, whereas one ligand histidine is in a loop following this helix and the other one is in a beta-strand.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-1312679,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-1324168,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-1330560,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-13771349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-13866633,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-1649622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-1846619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-1942029,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-2178268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-2824194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-2836423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-2849565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-4318312,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-6304038,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-708713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-7756569,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-8020495,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-8050583,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-8068678,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-8119391,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-8253767,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-8390373,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-8391869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-8393874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7638162-8395206
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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 |
Aug
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pubmed:issn |
0027-8424
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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 |
92
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7167-71
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7638162-Amino Acid Sequence,
pubmed-meshheading:7638162-Binding Sites,
pubmed-meshheading:7638162-Copper,
pubmed-meshheading:7638162-Electrochemistry,
pubmed-meshheading:7638162-Electron Transport Complex IV,
pubmed-meshheading:7638162-Models, Molecular,
pubmed-meshheading:7638162-Molecular Sequence Data,
pubmed-meshheading:7638162-Molecular Structure,
pubmed-meshheading:7638162-Spectrophotometry,
pubmed-meshheading:7638162-Spectrophotometry, Infrared,
pubmed-meshheading:7638162-Thermodynamics
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pubmed:year |
1995
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pubmed:articleTitle |
The CuA center of cytochrome-c oxidase: electronic structure and spectra of models compared to the properties of CuA domains.
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pubmed:affiliation |
Department of Physical Chemistry University of Technology, Göteborg, Sweden.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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