Covalent Modification of Catalytic Sites on Membrane-bound Beef Heart Mitochondrial ATPase by 2-Azido-adenine Nucleotides
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1994.01057.x/fullpdf
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1. 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
2. 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
3. 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
4. One of the non-exchangeable nucleotides of the mitochondrial F1-ATPase is bound at a β-subunit: evidence for a non-rotatory two-site catalytic mechanism;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1999-06
5. Analysis of the Nucleotide Binding Sites of ATP Synthase and Consequences for the Catalytic Mechanism;Frontiers of Cellular Bioenergetics;1999
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