Linked Life Data

17434442

Source:http://linkedlifedata.com/resource/pubmed/id/17434442

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2007-5-4
pubmed:abstractText
Following different reports on the stoichiometry and configuration of NO binding to mammalian and bacterial reduced cytochrome c oxidase aa(3) (CcO), we investigated NO binding and dynamics in the active site of beef heart CcO as a function of NO concentration, using ultrafast transient absorption and EPR spectroscopy. We find that in the physiological range only one NO molecule binds to heme a(3), and time-resolved experiments indicate that even transient binding to Cu(B) does not occur. Only at very high (approximately 2 mM) concentrations a second NO is accommodated in the active site, although in a different configuration than previously observed for CcO from Paracoccus denitrificans [E. Pilet, W. Nitschke, F. Rappaport, T. Soulimane, J.-C. Lambry, U. Liebl and M.H. Vos. Biochemistry 43 (2004) 14118-14127], where we proposed that a second NO does bind to Cu(B). In addition, in the bacterial enzyme two NO molecules can bind already at NO concentrations of approximately 1 microM. The unexpected differences highlighted in this study may relate to differences in the physiological relevance of the CcO-NO interactions in both species.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:volume
1767
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
387-92
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Accommodation of NO in the active site of mammalian and bacterial cytochrome c oxidase aa3.
pubmed:affiliation
Laboratoire d'Optique et Biosciences, CNRS, Ecole Polytechnique, F-91128 Palaiseau Cedex, France.
pubmed:publicationType
Journal Article