α-Aspartate 261 Is a Key Residue in Noncatalytic Sites of Escherichia coli F1-ATPase
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منابع مشابه
Nucleotide binding sites on beef heart mitochondrial F1-ATPase. Cooperative interactions between sites and specificity of noncatalytic sites.
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 contai...
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In the catalytic mechanism of ATP synthase, phosphate (Pi) binding and release steps are believed to be correlated to -subunit rotation, and Pi binding is proposed to be prerequisite for binding ADP in the face of high cellular [ATP]/[ADP] ratios. In x-ray structures, residue Asn-243 appears centrally located in the Pibinding subdomain of catalytic sites. Here we studied the role of Asn-243 in ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1995
ISSN: 0021-9258
DOI: 10.1074/jbc.270.36.21045