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• W2391363463 abstract "The structure and function of the F1F0ATP synthase have been studied by Xray crystallography, fluorescently labeled microscope, electron microscope after negative staining of specimens, monoclonal antibody, and so on. The results showed that the F1F0ATP synthase complexes are comprised of 8,9, and 16 different subunits respectively in Escherichia coli, chloroplasts and mitochondria, and that all Ftype ATP synthase have a similar structure. The globular F1 domain and the intrinsic membrane F0 domain linked by a central and peripheral stalk. One of the stalks belongs to the rotor and is built of γ and e subunits. The other stalk belongs to the stator and consists of subunits b2 (Ⅰ,Ⅱ) and δ. The γ subunit penetrates the catalytic (α3β3) domain and protrudes beneath it, interacting with a ring of c subunits in the membrane that drives rotation of the stalk during ATP synthesis. The F1F0ATP synthase catalyses the formation of ATP (adenosine triphosphate) from ADP (adenosine diphosphate) and Pi (inorganic phosphate) by using the energy of electrochemical proton gradient derived from electron transport." @default.
• W2391363463 created "2016-06-24" @default.
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• W2391363463 date "2003-01-01" @default.
• W2391363463 modified "2023-09-23" @default.
• W2391363463 title "Structure and function of supramolecular complex of F_1F_0-ATP synthase" @default.
• W2391363463 hasPublicationYear "2003" @default.
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