Source:http://linkedlifedata.com/resource/pubmed/id/21745457
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
10
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| pubmed:dateCreated |
2011-8-12
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| pubmed:abstractText |
The functional roles of the amino acid residues of the Cu(A) site in bovine cytochrome c oxidase (CcO) were investigated by utilizing hybrid quantum mechanics (QM)/molecular mechanics (MM) calculations. The energy levels of the molecular orbitals (MOs) involving Cu d(zx) orbitals unexpectedly increased, as compared with those found previously with a simplified model system lacking the axial Met residue (i.e., Cu(2)S(2)N(2)). This elevation of MO energies stemmed from the formation of the anti-bonding orbitals, which are generated by hybridization between the d(zx) orbitals of Cu ions and the p-orbitals of the S and O atoms of the axial ligands. To clarify the roles of the axial Met ligand, the inner-sphere reorganization energies of the Cu(A) site were computed, with the Met residue assigned to either the QM or MM region. The reorganization energy slightly increased when the Met residue was excluded from the QM region. The existing experimental data and the present structural modeling study also suggested that the axial Met residue moderately increased the redox potential of the Cu(A) site. Thus, the role of the Met may be to regulate the electron transfer rate through the fine modulation of the electronic structure of the Cu(A) "platform", created by two Cys/His residues coordinated to the Cu ions. This regulation would provide the optimum redox potential/reorganization energy of the Cu(A) site, and thereby facilitate the subsequent cooperative reactions, such as the proton pump and the enzymatic activity, of CcO. This article is part of a Special Issue entitled: Allosteric cooperativity in respiratory proteins.
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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 |
Oct
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| pubmed:issn |
0006-3002
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| pubmed:author | |
| pubmed:copyrightInfo |
Copyright © 2011 Elsevier B.V. All rights reserved.
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| pubmed:issnType |
Print
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| pubmed:volume |
1807
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1314-27
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| pubmed:meshHeading |
pubmed-meshheading:21745457-Amino Acid Sequence,
pubmed-meshheading:21745457-Animals,
pubmed-meshheading:21745457-Binding Sites,
pubmed-meshheading:21745457-Cattle,
pubmed-meshheading:21745457-Computational Biology,
pubmed-meshheading:21745457-Copper,
pubmed-meshheading:21745457-Electron Transport,
pubmed-meshheading:21745457-Electron Transport Complex IV,
pubmed-meshheading:21745457-Ligands,
pubmed-meshheading:21745457-Methionine,
pubmed-meshheading:21745457-Models, Chemical,
pubmed-meshheading:21745457-Models, Molecular,
pubmed-meshheading:21745457-Molecular Sequence Data,
pubmed-meshheading:21745457-Mutation,
pubmed-meshheading:21745457-Oxidation-Reduction,
pubmed-meshheading:21745457-Protein Structure, Tertiary,
pubmed-meshheading:21745457-Quantum Theory,
pubmed-meshheading:21745457-Sequence Homology, Amino Acid,
pubmed-meshheading:21745457-Thermodynamics
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| pubmed:year |
2011
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| pubmed:articleTitle |
A theoretical investigation of the functional role of the axial methionine ligand of the Cu(A) site in cytochrome c oxidase.
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| pubmed:affiliation |
University of Tsukuba, Tsukuba Science City, Ibaraki, Japan.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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