Catalytic cooperativity in the Ca2+-dependent ATPase activity of spinach chloroplast coupling factor (CF1)
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference42 articles.
1. ATP SYNTHASE (H+-ATPase): Results by Combined Biochemical and Molecular Biological Approaches
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4. Catalytic site occupancy during ATP hydrolysis by MF1-ATPase. Evidence for alternating high affinity sites during steady-state turnover.
Cited by 6 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. A bi-site mechanism for Escherichia coli F1-ATPase accounts for the observed positive catalytic cooperativity;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2009-08
2. Cooperativity between the enzymatic sites of F-1-ATPase revisited by the use of HPLC methods;Journal of Bioenergetics and Biomembranes;1998
3. Structure function relationship of vanadate bound to a single site in chloroplast CF1-ATPase as determined by X-ray absorption;Photosynthesis Research;1998
4. Unisite ATP hydrolysis by soluble Rhodospirillum rubrum F1–ATPase is accelerated by Ca2+;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1998-01
5. Protein and peptide inhibitors of the F1-ATPase;Biochemical Society Transactions;1995-11-01
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