Abstract
The energy transducing ATPase of mitochondria, chloroplasts, and bacteria is one of the most complex enzymes. It consists of at least ten different subunit polypeptides ranging in molecular weight from 60,000 to 8000 daltons. We have concentrated our efforts during the past few years on the smallest subunit of 8000 daltons, especially on its chemical characterization. This extremely hydrophobic polypeptide occurs in the complex as an oligomer, probably as a hexamer (Sebald et al., 1978) and is thus a major subunit, comprising about 10% of the total enzyme protein. Together with at least two further hydrophobic polypeptides it constitutes the membrane factor Fo (Sone et al., 1975; Sebald, 1977), which has been shown to exhibit the properties of a proton channel (Hinkle and Horstman, 1971; Okamoto et al., 1977).
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Sebald, W., Wachter, E. (1978). Amino Acid Sequence of the Putative Protonophore of the Energy-Transducing ATPase Complex. In: Schäfer, G., Klingenberg, M. (eds) Energy Conservation in Biological Membranes. Colloquium der Gesellschaft für Biologische Chemie, vol 29. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-81287-3_18
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DOI: https://doi.org/10.1007/978-3-642-81287-3_18
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