Abstract

The ATP synthase enzymes of the inner membranes of mitochondria, chloroplasts and of the bacterial cytoplasmic membrane, couple the energy of a transmembrane electrochemical proton gradient to the synthesis of ATP from ADP and inorganic phosphate. The general structural features of the enzyme are highly conserved from one organism to another. It is comprised of an integral membrane-spanning H+- translocating segment (F0 or factor O) and a peripheral membrane segment (F1 or factor 1) which contains the catalytic sites for ATP synthesis and hydrolysis. The F1 segment is comprised of five different polypeptide subunits designated α to e in order of decreasing molecular weight. The subunit stoichiometry is α3β3γ1δ1 and e1 (1).

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