Source:http://linkedlifedata.com/resource/pubmed/id/10876157
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
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| pubmed:dateCreated |
2000-10-19
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| pubmed:abstractText |
The bacterium, Vitreoscilla, produces a delta mu(Na+) across its membrane during respiration. A key enzyme for this function is the cytochrome bo terminal oxidase which, when incorporated into synthetic proteoliposomes, pumps Na(+) across the membrane upon the addition of a substrate. A Vitreoscilla cytochrome bo knock out (cyo(-)) mutant was isolated by transposon mutagenesis using pUT-mini-Tn5Cm. The membranes of this mutant lacked the characteristic 416 nm peak and 432 nm trough in CO difference spectra, which are clearly visible in spectra of the Vitreoscilla wild-type, but peaks at 627, 560, and 530 nm in reduced minus oxidized difference spectra indicate that cytochrome bd is still present. The specific NADH oxidase and ubiquinol-1 oxidase activities of the cyo(-) mutant membranes were less than those of Vitreoscilla wild-type and Escherichia coli membranes, and the stimulation of these activities of the mutant and E. coli membranes by 75 mM NaCl was approximately 50% less than that of Vitreoscilla wild-type membranes. The ubiquinol-1 oxidase activity of the cyo(-) mutant membranes was inhibited by 10 mM KCN to a lesser degree than that of the Vitreoscilla wild-type and E. coli membranes (50, 80, and 85%, respectively). This result is also consistent with the cyo(-) mutant membrane fragments containing only the cytochrome bd terminal oxidase, which is known to be less sensitive to KCN. Although the maximum respiration and growth of the cyo(-) mutant were less than those of the wild-type, this mutant is still capable of growing with cytochrome bd alone.
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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/Cytochrome b Group,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochromes,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Transposable Elements,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/NADH, NADPH Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/NADH oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Quinone Reductases,
http://linkedlifedata.com/resource/pubmed/chemical/Sodium,
http://linkedlifedata.com/resource/pubmed/chemical/Succinic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/cytochrome bo, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/ubiquinol-1 oxidase
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jul
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| pubmed:issn |
0021-924X
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
128
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
49-55
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| pubmed:dateRevised |
2007-12-19
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| pubmed:meshHeading |
pubmed-meshheading:10876157-Cell Division,
pubmed-meshheading:10876157-Cell Membrane,
pubmed-meshheading:10876157-Cytochrome b Group,
pubmed-meshheading:10876157-Cytochromes,
pubmed-meshheading:10876157-DNA Transposable Elements,
pubmed-meshheading:10876157-Escherichia coli Proteins,
pubmed-meshheading:10876157-Gene Silencing,
pubmed-meshheading:10876157-Genetic Engineering,
pubmed-meshheading:10876157-Multienzyme Complexes,
pubmed-meshheading:10876157-Mutation,
pubmed-meshheading:10876157-NADH, NADPH Oxidoreductases,
pubmed-meshheading:10876157-Quinone Reductases,
pubmed-meshheading:10876157-Sodium,
pubmed-meshheading:10876157-Succinic Acid,
pubmed-meshheading:10876157-Vitreoscilla
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| pubmed:year |
2000
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| pubmed:articleTitle |
Study of cytochrome bo function in Vitreoscilla using a cyo(-) knockout mutant.
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| pubmed:affiliation |
Division of Biology, Department of Biological, Chemical, and Physical Sciences, Illinois Institute of Technology, Chicago, IL 60616, USA.
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| pubmed:publicationType |
Journal Article
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