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Modulation of nucleotide binding to the catalytic sites of thermophilic F(1)-ATPase by the epsilon subunit: implication for the role of the epsilon subunit in ATP synthesis.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2009 Dec 11; Vol. 390 (2), pp. 230-4. Date of Electronic Publication: 2009 Sep 26. - Publication Year :
- 2009
-
Abstract
- Effect of epsilon subunit on the nucleotide binding to the catalytic sites of F(1)-ATPase from the thermophilic Bacillus PS3 (TF(1)) has been tested by using alpha(3)beta(3)gamma and alpha(3)beta(3)gammaepsilon complexes of TF(1) containing betaTyr341 to Trp substitution. The nucleotide binding was assessed with fluorescence quenching of the introduced Trp. The presence of the epsilon subunit weakened ADP binding to each catalytic site, especially to the highest affinity site. This effect was also observed when GDP or IDP was used. The ratio of the affinity of the lowest to the highest nucleotide binding sites had changed two orders of magnitude by the epsilon subunit. The differences may relate to the energy required for the binding change in the ATP synthesis reaction and contribute to the efficient ATP synthesis.
- Subjects :
- Adenosine Diphosphate chemistry
Adenosine Diphosphate metabolism
Adenosine Triphosphate metabolism
Catalytic Domain
Escherichia coli Proteins chemistry
Escherichia coli Proteins metabolism
Guanosine Diphosphate chemistry
Guanosine Diphosphate metabolism
Proton-Translocating ATPases chemistry
Adenosine Triphosphate biosynthesis
Bacillus enzymology
Proton-Translocating ATPases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1090-2104
- Volume :
- 390
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 19785990
- Full Text :
- https://doi.org/10.1016/j.bbrc.2009.09.092