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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1985-5-8
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pubmed:abstractText |
Papain treatment of the cytochrome b-c1 complex from beef heart results in partial proteolysis of core protein II, the iron-sulphur protein and the 15-kDa subunit. Under these conditions a significant inhibition of electron flow and complete suppression of proton translocation in the complex reconstituted into liposomes are observed. Kinetic experiments indicate a correlation between the digestion of core protein II and 15-kDa subunit and the suppression of proton translocation. The results suggest an active involvement of polypeptides of the complex in stabilizing the semiquinone species and/or providing pathways to exchange protons between bound quinone systems and aqueous phases.
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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 |
Mar
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
182
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
370-4
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2579851-Animals,
pubmed-meshheading:2579851-Cattle,
pubmed-meshheading:2579851-Electron Transport,
pubmed-meshheading:2579851-Electron Transport Complex III,
pubmed-meshheading:2579851-Ion Channels,
pubmed-meshheading:2579851-Kinetics,
pubmed-meshheading:2579851-Liposomes,
pubmed-meshheading:2579851-Multienzyme Complexes,
pubmed-meshheading:2579851-Myocardium,
pubmed-meshheading:2579851-NADH, NADPH Oxidoreductases,
pubmed-meshheading:2579851-Oxidation-Reduction,
pubmed-meshheading:2579851-Papain,
pubmed-meshheading:2579851-Peptide Fragments,
pubmed-meshheading:2579851-Protons,
pubmed-meshheading:2579851-Quinone Reductases
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pubmed:year |
1985
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pubmed:articleTitle |
Effect of papain digestion on redox-linked proton translocation in b-c1 complex from beef heart reconstituted into liposomes.
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pubmed:publicationType |
Journal Article
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