Source:http://linkedlifedata.com/resource/pubmed/id/12741819
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
19
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pubmed:dateCreated |
2003-5-13
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pubmed:abstractText |
Ubiquinone-2 (UQ-2) selectively labeled with (13)C (I =(1)/(2)) at either the position 1- or the 4-carbonyl carbon is incorporated into the ubiquinol oxidase bo(3) from Escherichia coli in which the native quinone (UQ-8) has been previously removed. The resulting stabilized anion radical in the high-affinity quinone-binding site (Q(H)(*)(-)) is investigated using multifrequency (9, 34, and 94 GHz) electron paramagnetic resonance (EPR) spectroscopy. The corresponding spectra reveal dramatic differences in (13)C hyperfine couplings indicating a strongly asymmetric spin density distribution over the quinone headgroup. By comparison with previous results on labeled ubisemiquinones in proteins as well as in organic solvents, it is concluded that Q(H)(*)(-) is most probably bound to the protein via a one-sided hydrogen bond or a strongly asymmetric hydrogen-bonding network. This observation is discussed with regard to the function of Q(H) in the enzyme and contrasted with the information available on other protein-bound semiquinone radicals.
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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/Coenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquinone,
http://linkedlifedata.com/resource/pubmed/chemical/coenzyme Q10,
http://linkedlifedata.com/resource/pubmed/chemical/duroquinol oxidase
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
42
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5632-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:12741819-Binding Sites,
pubmed-meshheading:12741819-Coenzymes,
pubmed-meshheading:12741819-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:12741819-Escherichia coli,
pubmed-meshheading:12741819-Hydrogen Bonding,
pubmed-meshheading:12741819-Kinetics,
pubmed-meshheading:12741819-Models, Molecular,
pubmed-meshheading:12741819-Oxidoreductases,
pubmed-meshheading:12741819-Static Electricity,
pubmed-meshheading:12741819-Ubiquinone
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pubmed:year |
2003
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pubmed:articleTitle |
Asymmetric binding of the high-affinity Q(H)(*)(-) ubisemiquinone in quinol oxidase (bo3) from Escherichia coli studied by multifrequency electron paramagnetic resonance spectroscopy.
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pubmed:affiliation |
Institut für Physikalische und Theoretische Chemie, J. W. Goethe Universität Frankfurt, Centre for Biological Magnetic Resonance, Frankfurt am Main, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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