ATP-hydrolysis in chloroplasts: Uni-site catalysis and evidence for heterogeneity of catalytic sites
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
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1. 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
2. Important subunit interactions in the chloroplast ATP synthase;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2000-05
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. Nucleotide-CF1 interactions and current views on the catalytic mechanism;Photosynthesis Research;1998
5. ATPase activity of thylakoid membranes in CTAB-hexanol-octane low water system;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1997-07
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