Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-6-19
pubmed:abstractText
The effect of the free radical nitric oxide (NO) on the activity of isolated cytochrome sigma oxidase was investigated by using ferrocytochrome sigma as an electron donor, and the system SNOG/DTT, which produces a steady-state NO concentration similar to that expected to be found in vivo. The initial electron entry into the heme a/Cu a center and the initial rate of the electron transfer between the two hemes were not affected by the presence of NO. Under our conditions, the rate of inhibition of cytochrome c oxidase was found to be dependent both on the SNOG (NO concentration) and on the ferrocytochrome c concentration (electron entry rate). The data confirm that NO binds exclusively at the binuclear center, and that the NO binding in these conditions requires the presence of an intermediate populated only in turnover. Accordingly, we found that the rate of inhibition is directly related to the electron entry rate. In addition, a residual activity seems to be present in cytochrome c oxidase in the presence of nitric oxide, suggesting that NO can act as an electron acceptor to cytochrome c oxidase in the presence of oxygen.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0162-0134
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
66
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
207-12
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
The inhibition of cytochrome c oxidase by nitric oxide using S-nitrosoglutathione.
pubmed:affiliation
Department of Biological and Chemical Sciences, University of Essex, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't