The Critical Electric Potential Difference for Photophosphorylation

Abstract

The physical meaning of the observed critical electric potential difference necessary for photophosphorylation is discussed. An interpretation of this phenomenon on the basis of the equilibrium thermodynamic formulation of the chemiosmotic hypothesis requires a reversible ATPase system. Contrary to this, ATP hydrolysis experiments seem to confirm that the Mg ++ ‐dependent ATPase system of class II‐chloroplasts is irreversible in the absence of SH‐compounds. This sheds doubt on the equilibrium thermodynamic interpretation of the critical electric potential difference for phosphorylation. However it can be shown, that the seeming irreversibility may be due to some trigger requirements of an intrinsically reversible ATPase system. This leads to an identification of the critical electric potential difference with the triggering level of the enzyme system. Two operational models for an ATPase system, whose activity is modulated by the electric potential difference, are derived. These account quantitatively for a set of experiments on the critical electric potential difference.