Abstract
F0F1 H+ATPase (or F-type ATPase) catalyzes ATP synthesis or hydrolysis coupling with proton translocation (for reviews, see Futai et al., 1989; Senior, 1990; Fillingame, 1990). The F-type ATPase of Escherichia coli is similar to those found in inner mitochondrial or chloroplast thylakoid membranes, and has contributed greatly to the understanding of this complicated enzyme. The catalytic site of the enzyme is in the P subunit or at the interface between the α and β subunits of the membrane extrinsic F1 sector. The proton pathway is formed from the a, b, and c subunits of the membrane intrinsic Fo sector. The γ, δ, and ε subunits of F1 are required functionally and structurally to connect the catalytic subunits to the Fo sector. The mechanism of ATP hydrolysis can be studied using purified F1 (F1 — ATPase).
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References
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© 1994 Springer-Verlag Berlin Heidelberg
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Iwamoto, A., Omote, H., Nakamoto, R.K., Maeda, M., Futai, M. (1994). F-type H+-ATPase: Catalysis and Proton Transport. In: Hirst, B.H. (eds) Molecular and Cellular Mechanisms of H+ Transport. NATO ASI Series, vol 89. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-79301-1_26
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