Aurovertin Fluorescence Changes of the Mitochondrial F1-ATPase during Multi- and Uni-site ATP Hydrolysis
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference31 articles.
1. Aurovertin, a Fluorescent Probe of Conformational Change in Beef Heart Mitochondrial Adenosine Triphosphatase
2. Energy-dependent Enhancement of Aurovertin Fluorescence
3. Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate enhancements resulting from cooperative interactions between multiple catalytic sites.
4. Adenine nucleotide binding sites on beef heart F1-ATPase. Evidence for three exchangeable sites that are distinct from three noncatalytic sites.
5. Action of the mitochondrial ATPase inhibitor protein on the Ca2+-ATPase of sarcoplasmic reticulum
Cited by 4 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. Effect of denaturants on multisite and unisite ATP hydrolysis by bovine heart submitochondrial particles with and without inhibitor protein;Archives of Biochemistry and Biophysics;2005-07
2. Inhibition by trifluoperazine of ATP synthesis and hydrolysis by particulate and soluble mitochondrial F1: Competition with H2PO 4 −;Journal of Bioenergetics and Biomembranes;1995-02
3. Interaction of beef-heart mitochondrial F1-ATPase with immobilized ATP in the presence of dimethylsulfoxide;Journal of Bioenergetics and Biomembranes;1992-10
4. The native mitochondrial F1-inhibitor protein complex carries out uni- and multisite ATP hydrolysis.;Journal of Biological Chemistry;1990-11
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