Linked Life Data

8226836

Source:http://linkedlifedata.com/resource/pubmed/id/8226836

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
31
pubmed:dateCreated
1993-11-29
pubmed:abstractText
We have studied the properties of beef heart mitochondrial F1 having inhibitory MgADP bound at one of the three catalytic sites and various levels of occupancy of the three noncatalytic nucleotide sites including zero, two, or three ADP/ATPs or two ADP/ATP plus one GTP. The properties examined include the rate of MgATP-dependent reactivation and the rate of increase in the fraction of F1 containing transiently bound intermediates. For each form of the enzyme tested, the rate of reactivation closely paralleled the rate of increase in the level of bound intermediates, indicating that when one catalytic site on F1 is blocked by inhibitory MgADP, the remaining two sites are incapable of residual uni- or bi-site activity. It was also found that the stability of the MgADP-inhibited complex decreases with full occupancy of the noncatalytic sites. This demonstrates that the noncatalytic sites modulate the properties of catalytic sites. Finally, it was found that the noncatalytic sites on mitochondrial F1 do not, as has long been believed, bind adenine nucleotides exclusively. Evidence is presented that both GTP and PPi bind tightly at noncatalytic sites.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
23179-85
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Nucleotide binding sites on beef heart mitochondrial F1-ATPase. Cooperative interactions between sites and specificity of noncatalytic sites.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, State University of New York Health Science Center, Syracuse 13210.
pubmed:publicationType
Journal Article, In Vitro, Research Support, U.S. Gov't, P.H.S.