The role of tightly bound ADP on chloroplast ATPase.
Open Access
- 1 October 1985
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 260 (24) , 13088-13094
- https://doi.org/10.1016/s0021-9258(17)38842-7
Abstract
No abstract availableThis publication has 44 references indexed in Scilit:
- Tightly bound adenosine diphosphate, which inhibits the activity of mitochondrial F1‐ATPase, is located at the catalytic site of the enzymeFEBS Letters, 1985
- Methanol-induced release of tightly bound adenine nucleotides from thylakoid-associated CF1Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1984
- Activation of ATPase of spinach coupling factor 1. Release of tightly bound ADP from the soluble enzymeEuropean Journal of Biochemistry, 1984
- The Mr‐value of chloroplast coupling factor 1FEBS Letters, 1983
- Activity and conformational changes in chloroplast coupling factor induced by ion binding: formation of a magnesium-enzyme-phosphate complexBiochemistry, 1983
- Mechanism of ATP synthesis and coupled proton transport: studies with purified chloroplast coupling factorTrends in Biochemical Sciences, 1983
- Modulation of the chloroplast ATPase by tight binding of nucleotidesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1982
- Kinetic analysis of light‐dependent exchange of adenine nucleotides on chloroplast coupling factor CF1FEBS Letters, 1979
- Characterization of nucleotide binding sites on chloroplast coupling factor 1Biochemistry, 1975
- On the mechanism of activation of the ATPase in chloroplastsBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1974