Abstract
The phosphorylation reaction catalyzed by a membrane bound ATPase must be endothermic when driven by a transmembrane pH difference. This fundamental property has not been recognized in current discussions concerning the chemiosmotic mechanism of phosphorylation, although it can serve as a direct indicator of the participation of a pH gradient in the process. This note presents a description of the thermodynamics of a transmembranal electrochemical potential gradient either when it is dissipated by a non specific leakage, or when it drives phosphorylation. As an illustration, it is shown that a temperature decrease of 0.01°C is to be expected in a typical acid-base driven phosphorylation in chloroplasts.
Published Version
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