Inhibition of mitochondrial F1-ATPase activity by binding of (2-azido-)ADP to a slowly exchangeable non-catalytic nucleotide binding site
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
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1. ATP Synthase and the Actions of Inhibitors Utilized To Study Its Roles in Human Health, Disease, and Other Scientific Areas;Microbiology and Molecular Biology Reviews;2008-12
2. Covalent modification of the non-catalytic sites of the H + -ATPase from chloroplasts with 2-azido-[α- 32 P]ATP and its effect on ATP synthesis and ATP hydrolysis;Biochimica et Biophysica Acta (BBA) - Biomembranes;2001-02
3. Covalent modification of the catalytic sites of the H+-ATPase from chloroplasts with 2-nitreno-ADP. Modification of the catalytic site 1 (tight) and catalytic sites 1 and 2 together impairs both uni-site and multi-site catalysis of ATP synthesis and ATP hydrolysis;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2000-07
4. Analysis of the nucleotide binding sites of mitochondrial ATP synthase provides evidence for a two-site catalytic mechanism;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2000-05
5. Characterization of Nucleotide Binding Sites of the Isolated H+-ATPase from Spinach Chloroplasts, CF0F1;Archives of Biochemistry and Biophysics;2000-04
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