Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1993-5-19
|
pubmed:abstractText |
We have detected weak absorption bands in the near infra-red region of reduced mammalian cytochrome c oxidase, analogous to those that we have recently reported to be present in the bacterial cytochrome o (Ingledew, W.J., Bacon, M. and Rich, P.R. (1992) FEBS Lett. 305, 167-170). The major band is centred at 784 nm and has an sigma mM-1.cm-1 of around 0.1. It is shifted to 760 nm in the carbon monoxide compound and is absent in the reduced cyanide complex. We attribute it to a charge transfer band of ferrohaem a3, equivalent to the 'band III' or 'conformational band' of haemoglobin.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
0014-5793
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
6
|
pubmed:volume |
305
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
171-3
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:1338593-Animals,
pubmed-meshheading:1338593-Carbon Monoxide,
pubmed-meshheading:1338593-Cattle,
pubmed-meshheading:1338593-Electron Transport Complex IV,
pubmed-meshheading:1338593-Oxidation-Reduction,
pubmed-meshheading:1338593-Photolysis,
pubmed-meshheading:1338593-Spectrophotometry,
pubmed-meshheading:1338593-Spectrophotometry, Infrared
|
pubmed:year |
1992
|
pubmed:articleTitle |
Detection of a near infra-red absorption band of ferrohaem a3 in cytochrome c oxidase.
|
pubmed:affiliation |
Glynn Research Institute, Bodmin, Cornwall, UK.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|