Interaction of the chloroplast ATP synthetase with the photoreactive nucleotide 3′-O -(4-benzoyl)benzoyl adenosine 5'-diphosphate
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(83)80973-9/fullpdf
Reference26 articles.
1. Energy Transduction in Chloroplasts: Structure and Function of the ATPase Complex
2. Role of tight nucleotide binding in the regulation of the chloroplast ATP synthetase activities
3. Modulation of the chloroplast ATPase by tight binding of nucleotides
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2. Analysis of the nucleotide binding sites of mitochondrial ATP synthase provides evidence for a two-site catalytic mechanism;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2000-05
3. Analysis of the Nucleotide Binding Sites of ATP Synthase and Consequences for the Catalytic Mechanism;Frontiers of Cellular Bioenergetics;1999
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5. Modification of domains of α and β subunits of F1-ATPase from the thermophylic bacterium PS3, in their isolated and associated forms, by 3′-O-(4-benzoyl)benzoyl adenosine 5′-triphosphate (BzATP);Journal of Bioenergetics and Biomembranes;1996-12
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