Abstract
WE have recently reported that when suspensions of intact rat liver mitochondria hydrolyse ATP, oxidize succinate, or oxidize β-hydroxybutyrate, protons are translocated (written →H+) outwards through the mitochondrial membrane with stoichiometries closely approximating to →H+/P = 2, →H+/O = 4 and →H+/O = 6 respectively1. These observations are in close accord with the requirements of the chemiosmotic hypothesis, according to which electron transport and phosphorylation are coupled by the proton current flowing cyclically through the respiratory chain and reversible ATPase systems across the cristae membrane2; but they could also be explained according to the chemical hypothesis, by invoking a proton pump driven by hydrolysis of X ∼ I, either directly, or via the ‘W complex’ suggested by Lardy, Connelly and Johnson3. We have, therefore, sought more crucial experimental tests of the alternative hypotheses.
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References
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MITCHELL, P., MOYLE, J. Evidence discriminating between the Chemical and the Chemiosmotic Mechanisms of Electron Transport Phosphorylation. Nature 208, 1205–1206 (1965). https://doi.org/10.1038/2081205a0
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DOI: https://doi.org/10.1038/2081205a0
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