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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
1990-3-30
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| pubmed:abstractText |
Two terminal oxidase complexes, cytochrome b-562-o complex and cytochrome b-558-d complex, are isolated in highly purified forms which show ubiquinol oxidase activities. From the result of steady-state kinetics of cytochromes in the membrane and E'm values of purified cytochromes, we propose a branched arrangement of the late exponential phase of aerobic growth, as shown in Fig. 10. Cytochrome b-556 is reduced by several dehydrogenases and the gene for this cytochrome (cybA) is located in the sdh gene cluster. Recently, we found another low-potential b-type cytochrome, cytochrome b-561 (Em' = 20 mV), which is also reduced by dehydrogenases. The position of this new cytochrome in the aerobic respiratory chain is under investigation. Two terminal oxidase complexes branch at the site of ubiquinone-8, and the Km value for oxygen of the purified cytochrome b-558-d complex is about 8-fold lower than that of the purified cytochrome b-562-o complex when ubiquinol-1 is used as substrate. This result is consistent with the idea that the cytochrome b-558-d complex is synthesized as an alternative oxidase for more efficient utilization of oxygen at low oxygen concentration. Thus, E. coli cells can maintain efficient oxidative energy conservation over a wide range of oxygen pressures by simply changing the contents of the two terminal oxidases, each of which functions as a coupling site.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome b Group,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochromes,
http://linkedlifedata.com/resource/pubmed/chemical/Electron Transport Chain Complex...,
http://linkedlifedata.com/resource/pubmed/chemical/Electron Transport Complex IV,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NADPH Oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/cytochrome b558,
http://linkedlifedata.com/resource/pubmed/chemical/cytochrome b562, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/cytochrome bd terminal oxidase...,
http://linkedlifedata.com/resource/pubmed/chemical/cytochrome o oxidase
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| pubmed:status |
MEDLINE
|
| pubmed:issn |
0076-6879
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
126
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
94-113
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:2856144-Cell Membrane,
pubmed-meshheading:2856144-Chromatography, Gel,
pubmed-meshheading:2856144-Chromatography, Ion Exchange,
pubmed-meshheading:2856144-Cytochrome b Group,
pubmed-meshheading:2856144-Cytochromes,
pubmed-meshheading:2856144-Electron Transport Chain Complex Proteins,
pubmed-meshheading:2856144-Electron Transport Complex IV,
pubmed-meshheading:2856144-Escherichia coli,
pubmed-meshheading:2856144-Escherichia coli Proteins,
pubmed-meshheading:2856144-Kinetics,
pubmed-meshheading:2856144-NADPH Oxidase,
pubmed-meshheading:2856144-Oxidoreductases,
pubmed-meshheading:2856144-Oxygen Consumption
|
| pubmed:year |
1986
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| pubmed:articleTitle |
Purification and properties of two terminal oxidase complexes of Escherichia coli aerobic respiratory chain.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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