rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2
|
pubmed:dateCreated |
1997-10-21
|
pubmed:abstractText |
The vectorial nature of redox Bohr effects (redox-linked pK shifts) in cytochrome c oxidase from bovine heart incorporated in liposomes has been analyzed. The Bohr effects linked to oxido-reduction of heme a and CuB display membrane vectorial asymmetry. This provides evidence for involvement of redox Bohr effects in the proton pump of the oxidase.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Sep
|
pubmed:issn |
0014-5793
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
8
|
pubmed:volume |
414
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
414-8
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:9315731-Animals,
pubmed-meshheading:9315731-Carbon Monoxide,
pubmed-meshheading:9315731-Cattle,
pubmed-meshheading:9315731-Copper,
pubmed-meshheading:9315731-Electron Transport Complex IV,
pubmed-meshheading:9315731-Heme,
pubmed-meshheading:9315731-Hydrogen-Ion Concentration,
pubmed-meshheading:9315731-Kinetics,
pubmed-meshheading:9315731-Liposomes,
pubmed-meshheading:9315731-Mitochondria, Heart,
pubmed-meshheading:9315731-Oxidation-Reduction
|
pubmed:year |
1997
|
pubmed:articleTitle |
Vectorial nature of redox Bohr effects in bovine heart cytochrome c oxidase.
|
pubmed:affiliation |
Institute of Medical Biochemistry and Chemistry, University of Bari, Italy.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|