On the Structure of the ATP-Synthase from Chloroplasts

Böttcher, B.; Lücken, Uwe; Boekema, E. J.; Gräber, P.

doi:10.1007/978-94-009-0511-5_444

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On the Structure of the ATP-Synthase from Chloroplasts

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Böttcher, B.
Fritz Haber Institute, Max Planck Society;

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Lücken, Uwe
Fritz Haber Institute, Max Planck Society;

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Citation

Böttcher, B., Lücken, U., Boekema, E. J., & Gräber, P. (1990). On the Structure of the ATP-Synthase from Chloroplasts. In M. Baltscheffsky (Ed.), Current Research in Photosynthesis: Proceedings of the VIIIth International Conference on Photosynthesis Stockholm, Sweden, August 6–11, 1989 (pp. 1939-1942). Dordrecht: Springer.

Cite as: https://hdl.handle.net/21.11116/0000-0006-9415-B

Abstract

The H⁺-translocating ATPase (“ATP-synthase”) from chloroplasts is a membrane-bound enzyme which can couple a transmembrane proton transport with ATP synthesis/hydrolysis. The enzyme has a hydrophobic, membrane-integrated part, CF0, which is supposed to act as a proton channel through the membrane and a hydrophilic part, CF1 which contains the nucleotide-binding sites. The CF2 part contains five different subunits with the stoichiometry α₃β₃γδε, the CF_o part contains four different subunits with the stoichiometry I, II, III₁₂, IV However, there is no general agreement about the subunit stoichiometry up to now.