Abstract
According to Mitchell’s chemiosmotic theory of energy coupling, there are special enzymic systems carrying out translocation of electrons or protons across biological membranes [ 1 ] . Such a translocation should include the stages of electron (proton) transfer through a water-lipid interface, the processes being catalyzed (a) by certain enzymes operating in the energy coupling sites of the respiratory and photosynthetic redox chains, and (b) by H+-ATPase. In this paper, we shall report a method of investigation of the enzyme-mediated charge transfer across a water-lipid interface. The method consists in the measurement of the Volta potential difference between an octane and water solution, containing the enzyme system studied. Positive charging of the octane phase was found to be induced by soluble mitochondrial ATPase (Fr) in an ATP-dependent fashion, or by bacteriorhodopsin from Halobacterium halobium in a light-dependent fashion. In both cases, a lipid-soluble proton acceptor proved to be necessary. Cytochrome oxidase and succinate-cytochrome c-reductase were shown to carry out negative charging of octane if a lipid-soluble electron acceptor and water soluble elec-
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