Source of Rapidly Labeled ATP Tightly Bound to Non-catalytic Sites on the Chloroplast ATP Synthetase
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1982.tb06746.x/fullpdf
Reference27 articles.
1. The interactions of coupling ATPases with nucleotides
2. Structure of oxidative- and photo-phosphorylation coupling factor complexes
3. Energy Transduction in Chloroplasts: Structure and Function of the ATPase Complex
4. Energy-dependent release of adenine nucleotides tightly bound to chloroplast coupling factor CF1
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1. Localized firefly luciferase probes ATP at the surface of mitochondria;Journal of Bioenergetics and Biomembranes;1997
2. From uni-site to multi-site ATP synthesis in thylakoid membranes;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1993-09
3. The binding change mechanism for ATP synthase — Some probabilities and possibilities;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1993-01
4. Evidence that energization of the chloroplast ATP synthase favors ATP formation at the tight binding catalytic site and increases the affinity for ADP at another catalytic site.;Journal of Biological Chemistry;1993-01
5. An attempt to discriminate catalytic and regulatory proton binding sites in membrane-bound, thiol-reduced chloroplast ATPase;Biochemistry;1992-05
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