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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
16
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pubmed:dateCreated |
1992-7-6
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pubmed:abstractText |
The regulation of the membrane-bound H(+)-ATPase from the photosynthetic bacterium Rhodobacter capsulatus was investigated. In the presence of uncouplers the rate of ATP hydrolysis was about 40 mM ATP/M bacteriochlorophyll (Bchl)/s. Without uncouplers this rate increased and if, additionally, the chromatophores were illuminated, it was almost doubled. If uncouplers were added shortly after illumination, the rate increased to 300-350 mM ATP/M Bchl/s. Obviously, energization of the membrane leads to the formation of a metastable, active state of the H(+)-ATPase. The maximal rate of ATP hydrolysis can be measured only when first all H(+)-ATPases are activated by delta mu H+ and when the delta mu H+ is abolished in order to release its back pressure on the hydrolysis rate. The half-life time of the metastable state in the absence of delta mu H+ is about 30 s. It is increased by 3 mM Pi to about 80 s and it is decreased by 1 mM ADP to about 15 s. Quantitatively, the fraction of active H(+)-ATPases shows a sigmoidal dependence on pHin (at constant pHout) and the magnitude of delta psi determines the maximal fraction of enzymes which can be activated: delta pH and delta psi are not equivalent for the activation process.
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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 |
Jun
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
267
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11057-63
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1534558-Adenine Nucleotides,
pubmed-meshheading:1534558-Enzyme Activation,
pubmed-meshheading:1534558-Enzyme Stability,
pubmed-meshheading:1534558-Hydrogen-Ion Concentration,
pubmed-meshheading:1534558-Hydrolysis,
pubmed-meshheading:1534558-Light,
pubmed-meshheading:1534558-Membrane Potentials,
pubmed-meshheading:1534558-Phosphates,
pubmed-meshheading:1534558-Proton-Translocating ATPases,
pubmed-meshheading:1534558-Rhodobacter capsulatus
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pubmed:year |
1992
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pubmed:articleTitle |
Activation of the H(+)-ATP synthase in the photosynthetic bacterium Rhodobacter capsulatus.
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pubmed:affiliation |
Max-Volmer Institut, Technische Universität Berlin, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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