Linked Life Data

3024904

Source:http://linkedlifedata.com/resource/pubmed/id/3024904

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1987-2-11
pubmed:abstractText
The ubiquinol-cytochrome c oxidoreductase (bc1 complex, EC 1.10.2.2) has been isolated from the heart mitochondria of beef, chicken, turkey, duck and tuna with an identical procedure. The polypeptide composition of the different complexes, compared using SDS-polyacrylamide gel electrophoresis, shows that the three subunits carrying the prosthetic groups of the enzyme are highly conserved in all species. Also the large subunits I and II (core proteins) and band VI appear to be conserved in structure, while subunits VII and VIIa show a most remarkable structural variation in the various complexes. The steady-state ubiquinol-cytochrome c reductase analysis of the active enzymes indicates that all the bc1 complexes follow essentially a ping-pong mechanism, with the cytochrome c substrate displaying a partial competitive inhibition vs the ubiquinol substrate. The cytochrome c specificity of the reductase activity clearly is different in the various bc1 complexes, whereas the quinol specificity appears to be identical in all the enzymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0305-0491
pubmed:author
pubmed:issnType
Print
pubmed:volume
85
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
543-52
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Comparative biochemistry of the ubiquinol-cytochrome c oxidoreductase (EC 1.10.2.2) isolated from different heart mitochondria.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't