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Mitochondrial ATP Synthase: Structure, Biogenesis and Pathology

  • Chapter
Book cover Organellar Proton-ATPases

Part of the book series: Molecular Biology Intelligence Unit ((MBIU))

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Abstract

Mitochondrial ATP synthase catalyses probably the most crucial enzymatic reaction for aerobic, eukaryotic cells, namely oxidative phosphorylation, driven by the proton gradient created by the mitochondrial electron transfer chain. The enzyme is also capable, under defined physiological circumstances, of catalyzing the reverse reaction, namely the energization of the inner mitochondrial membrane at the expense of ATP. For this reason, and because ATP hydrolysis is usually much easier to assay than proton-driven ATP synthesis, the enzyme is often referred to as the mitochondrial ATPase or H+-ATPase, or as the F1F0 ATPase, after the names given to the two major sectors of the enzyme complex: the hydrophilic F1 sector, with intrinsic ATPase activity, and the hydrophobic F0 sector, which constitutes the proton channel through the inner mitochondrial membrane.

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Jacobs, H.T. (1995). Mitochondrial ATP Synthase: Structure, Biogenesis and Pathology. In: Organellar Proton-ATPases. Molecular Biology Intelligence Unit. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-22265-2_5

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