Modulation by divalent metal ions of the autocatalytic reactivity of adenosine triphosphatase from chloroplasts
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00516a042
Reference25 articles.
1. On the mechanism of activation of the ATPase in chloroplasts
2. Effects of Pi and ADP on ATPase activity in chloroplasts
3. Control of kinetic changes in ATPase activity of soluble coupling factor 1 from chloroplasts
4. Partial resolution of the enzymes catalyzing photophosphorylation. XV. Approaches to the active site of coupling factor I.
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1. Structure function relationship of vanadate bound to a single site in chloroplast CF1-ATPase as determined by X-ray absorption;Photosynthesis Research;1998
2. Differences between Two Tight ADP Binding Sites of the Chloroplast Coupling Factor 1 and Their Effects on ATPase Activity;Journal of Biological Chemistry;1996-08
3. Adenine nucleotide-binding sites on mitochondrial F1-ATPase: Studies of the inactive complex formed upon binding ADP at a catalytic site;Archives of Biochemistry and Biophysics;1992-06
4. Characteristics of the combination of inhibitory magnesium and azide with the F1 ATPase from chloroplasts;Biochemistry;1991-08-27
5. The characteristics and effect on catalysis of nucleotide binding to noncatalytic sites of chloroplast F1-ATPase;Journal of Biological Chemistry;1991-06
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