Binding and hydrolysis of 2-azido-ATP and 8-azido-ATP by isolated mitochondrial F1: Characterisation of high-affinity binding sites
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference36 articles.
1. Recent developments on structural and functional aspects of the F1 sector of H+-linked ATPases
2. The number and localisation of adenine nucleotide-binding sites in beef-heart mitochondrial ATPase (F1) determined by photolabelling with 8-azido-ATP and 8-azido-ADP
3. Adenine nucleotide binding sites on beef heart F1-ATPase. Evidence for three exchangeable sites that are distinct from three noncatalytic sites.
4. Total number and differentiation of nucleotide binding sites on mitochondrial F1-ATPase. An approach by photolabeling and equilibrium binding studies
5. Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate enhancements resulting from cooperative interactions between multiple catalytic sites.
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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. Covalent modification of the catalytic sites of the H+-ATPase from chloroplasts, CF0F1, with 2-azido-[α-32P]ADP: modification of the catalytic site 2 (loose) and the catalytic site 3 (open) impairs multi-site, but not uni-site catalysis of both ATP synthesis and ATP hydrolysis;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2000-01
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