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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1991-7-24
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pubmed:abstractText |
The effect of inhibitors of proton pumps, of uncouplers and of permeant ions on the relationship between input force, delta mu H+, and output flows of the ATPase, redox and transhydrogenase H(+)-pumps in submitochondrial particles was investigated. It is concluded that: (1) The decrease of output flow of the transhydrogenase proton pump, defined as the rate of reduction of NADP+ by NADH, is linearily correlated with the decrease of input force, delta mu H+, in an extended range of delta mu H+, independently of whether the H(+)-generating pump is the ATPase or a redox pump, or whether delta mu H+ is depressed by inhibitors of the H(+)-generating pump such as oligomycin or malonate, or by uncouplers. (2) The output flows of the ATPase and of the site I redox H(+)-pumps exhibit a steep dependence on delta mu H+. The flow-force relationships differ depending on whether the depression of delta mu H+ is induced by inhibitors of the H(+)-generating pump, by uncouplers or by lipophilic anions. (3) With the ATPase as H(+)-consuming pump, at equivalent delta mu H+ values, the output flow is more markedly inhibited by malonate than by uncouplers; the latter, however, are more inhibitory than lipophilic anions such as ClO4-. With redox site I as proton-consuming pump, at equivalent delta mu H+ values, the output flow is more markedly inhibited by oligomycin than by uncouplers; again, uncouplers are more inhibitory than ClO4-. (4) The results provide further support for a delocalized interaction of transhydrogenase with other H(+)-pumps.
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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/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/NADP,
http://linkedlifedata.com/resource/pubmed/chemical/Oligomycins,
http://linkedlifedata.com/resource/pubmed/chemical/Protons,
http://linkedlifedata.com/resource/pubmed/chemical/Succinates,
http://linkedlifedata.com/resource/pubmed/chemical/Succinic Acid
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
1058
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
297-303
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pubmed:dateRevised |
2003-11-14
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pubmed:meshHeading |
pubmed-meshheading:1646634-Adenosine Triphosphate,
pubmed-meshheading:1646634-Animals,
pubmed-meshheading:1646634-Cattle,
pubmed-meshheading:1646634-Energy Metabolism,
pubmed-meshheading:1646634-Mitochondria, Heart,
pubmed-meshheading:1646634-NAD,
pubmed-meshheading:1646634-NADP,
pubmed-meshheading:1646634-Oligomycins,
pubmed-meshheading:1646634-Protons,
pubmed-meshheading:1646634-Submitochondrial Particles,
pubmed-meshheading:1646634-Succinates,
pubmed-meshheading:1646634-Succinic Acid
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pubmed:year |
1991
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pubmed:articleTitle |
Flow-force relationships during energy transfer between mitochondrial proton pumps.
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pubmed:affiliation |
CNR Unit for the Physiology of Mitochondria, University of Padova, Italy.
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pubmed:publicationType |
Journal Article
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