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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1981-6-23
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pubmed:abstractText |
The electron transport chain was studied in the obligate methane oxidizing culture of Methylococcus thermophilus during the oxidation of methanol (the source of carbon) which is an oxidized derivative of methane as well as during the oxidation of hydroxylamine which is an intermediate in the oxidation of ammonium (the source of nitrogen) by Mc. thermophilus cells. Cytochromes a, b and c are involved in electron transport. Cytochrome cco and cytochrome c554 have been isolated from the cell-free extract of Mc. thermophilus and purified. A scheme for electron transport operating in the oxidation of methanol and hydroxylamine is suggested on the basis of studying the characteristics of these cytochromes. Cytochrome a was shown to be a component of terminal oxidase. Cytochromes b are connected with membranes and also found in the composition of hydroxylamine oxidase. Cytochrome cco and, possibly, terminal oxidase (cytochromes a) are involved, in the oxidation of CH3OH by methanol dehydrogenase, in electron transport; cytochrome c554 as well as cytochrome b and c in the composition of hydroxylamine oxidase participate in electron transport in the oxidation of NH2OH by hydroxylamine oxidase. The characteristics of the electron transport system in Mc. thermophilus are discussed.
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pubmed:language |
rus
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alcohol Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Ammonia,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochromes,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxylamines,
http://linkedlifedata.com/resource/pubmed/chemical/Methanol,
http://linkedlifedata.com/resource/pubmed/chemical/NADH Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/alcohol dehydrogenase (acceptor),
http://linkedlifedata.com/resource/pubmed/chemical/hydroxylamine oxidase
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pubmed:status |
MEDLINE
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pubmed:issn |
0026-3656
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
50
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
13-20
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7012552-Alcohol Oxidoreductases,
pubmed-meshheading:7012552-Ammonia,
pubmed-meshheading:7012552-Cytochromes,
pubmed-meshheading:7012552-Electron Transport,
pubmed-meshheading:7012552-Halobacteriaceae,
pubmed-meshheading:7012552-Hydroxylamines,
pubmed-meshheading:7012552-Methanol,
pubmed-meshheading:7012552-NADH Dehydrogenase,
pubmed-meshheading:7012552-Oxidoreductases,
pubmed-meshheading:7012552-Spectrum Analysis
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pubmed:articleTitle |
[Electron transport chain in a thermophilic methane-oxidizing culture of Methylococcus thermophilus].
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pubmed:publicationType |
Journal Article,
English Abstract
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