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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1988-5-11
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pubmed:abstractText |
A model is proposed for the respiratory adaptation to falling oxygen concentration during growth of the microaerophilic bacterium Campylobacter mucosalis. During the early stages of growth, the oxidation of formate is a two-stage branched process involving the production of H2O2 followed by its peroxidatic removal. In later stages of growth, at lower oxygen concentrations, the predominant electron flow is linear to a membrane-bound cytochrome-c oxidase which reduces O2 directly to H2O. Several components of this model have been investigated. H2O2 was produced during formate oxidation and accumulated when electron transfer to the cytochrome-c peroxidase was inhibited. A cytochrome c-553, of the Class 1 types, was purified and shown to be the specific electron donor to both the peroxidase and the membrane-bound oxidase. The levels of this cytochrome c and of the peroxidase were higher in cells harvested early in growth. In later stages of growth, the activity of the membrane-bound oxidase increased. Proton pumping across the membrane was detected with either H2O2 or oxygen as terminal electron acceptor. The novel energy-conserving role of H2O2 in this catalase-negative bacterium is discussed in relation to its microaerophilic nature.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochrome c Group,
http://linkedlifedata.com/resource/pubmed/chemical/Electron Transport Complex IV,
http://linkedlifedata.com/resource/pubmed/chemical/Formic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxidases,
http://linkedlifedata.com/resource/pubmed/chemical/cytochrome C-552,
http://linkedlifedata.com/resource/pubmed/chemical/cytochrome c553,
http://linkedlifedata.com/resource/pubmed/chemical/formic acid
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
933
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
114-23
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pubmed:dateRevised |
2009-9-29
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pubmed:meshHeading |
pubmed-meshheading:2831975-Adaptation, Physiological,
pubmed-meshheading:2831975-Aerobiosis,
pubmed-meshheading:2831975-Bacterial Proteins,
pubmed-meshheading:2831975-Campylobacter,
pubmed-meshheading:2831975-Cytochrome c Group,
pubmed-meshheading:2831975-Electron Transport,
pubmed-meshheading:2831975-Electron Transport Complex IV,
pubmed-meshheading:2831975-Formic Acids,
pubmed-meshheading:2831975-Hydrogen Peroxide,
pubmed-meshheading:2831975-Oxygen,
pubmed-meshheading:2831975-Peroxidases
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pubmed:year |
1988
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pubmed:articleTitle |
The microaerophilic respiration of Campylobacter mucosalis.
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pubmed:affiliation |
Biochemistry Unit, Royal (Dick) School of Veterinary Studies, University of Edinburgh, U.K.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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