It is shown that the "elementary act" of synthesis of ATP from ADP and inorganic phosphate in the energy-transforming structures of the mitochondria, chloroplasts and chromatophores does not require the presence of closed membrane vesicles, membrane residues and the F1 component of H+ ATP: it is realized through the quite rapid deprotonation of some acid groups of the F1H+ATP coupling factor as a result of which the enzyme is in a conformationally non-equilibrium state (the presence of "surplus" negative charges in the still unchanged protein globule). It has been established that the energy-acceptor act of ATP synthesis, i.e. release of the strongly bound ATP molecule into the aqueous phase occurs in the course of relaxation of this non-equilibrium state. It is concluded that closed membrane vesicles are necessary for the periodic return of the enzyme to the initial state with protonated acid groups ensuring the possibility of repeated synthesis of ATP in steady and quasisteady conditions. The energetics and possible schemes of this process are examined in detail in experiments on ATP synthesis in closed membrane vesicles during the formation of an artificial transmembrane pH gradient and also in the steady state on oxidative and photo-phosphorylation.
|Number of pages||16|
|Publication status||Published - Dec 1 1987|
ASJC Scopus subject areas