Linked Life Data

3007206

Source:http://linkedlifedata.com/resource/pubmed/id/3007206

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1986-5-7
pubmed:abstractText
The slow increase of a cyanide-induced optical change at 437 nm following rapid cyanide inhibition of cytochrome oxidase has been followed as a function of the number of electrons donated from ferrocytochrome c to cytochrome a and CuA. The initial rate of optical change is a parabolic function of this number. The results have been analyzed in terms of a model where addition of electrons causes a conformational transition allowing rapid cyanide binding. The binding is followed by a slow intramolecular responsible for the optical change. The analysis demonstrates that only molecules with both cytochrome a and CuA reduced can undergo the conformational change, which is suggested to be involved in the proton-pump mechanism of the oxidase.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
198
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
125-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Two-electron reduction of cytochrome c oxidase triggers a conformational transition.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't