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- [23] 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-BIOENERGETICS, 2000, 1459 (01): : 202 - 217
- [24] Regulation of F0F1 ATP synthase:: Subunit epsilon C-terminal domain is involved in inhibition by ADP and in activation by protonmotive force. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 2006, : 303 - 303
- [30] 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-BIOENERGETICS, 2000, 1456 (2-3): : 77 - 98