When beef-heart mitochondrial F1-ATPase is inhibited by inhibitor protein a nucleotide is trapped in one of the catalytic sites
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1991.tb16246.x/fullpdf
Reference48 articles.
1. A Naturally Occurring Inhibitor of Mitochondrial Adenosine Triphosphatase
2. Regulation of the mitochondrial ATP synthase/ATPase complex
3. Radiolabeling of natural adenosine triphosphatase inhibitor with phenyl[14C]isothiocyanate and study of its interaction with mitochondrial adenosine triphosphatase. Localization of inhibitor binding sites and stoichiometry of binding
4. Binding of mitochondrial ATPase from ox heart to its naturally occurring inhibitor protein: Localization by antibody binding
5. Binding of dicyclohexylcarbodiimide to a native F1-ATPase - inhibitor protein complex isolated from bovine heart mitochondria
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2. Insight into the Bind−Lock Mechanism of the Yeast Mitochondrial ATP Synthase Inhibitory Peptide;Biochemistry;2007-06-27
3. Rapid hydrolysis of ATP by mitochondrial F1-ATPase correlates with the filling of the second of three catalytic sites;Proceedings of the National Academy of Sciences;2005-09-19
4. Interconversion Between Dimers and Monomers of Endogenous Mitochondrial F1-Inhibitor Protein Complexes and the Release of the Inhibitor Protein. Spectroscopic Characteristics of the Complexes;Journal of Bioenergetics and Biomembranes;2004-12
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