Abstract <p>F<sub>o</sub>∙F<sub>1</sub> ATP synthases/ATPases (F<sub>o</sub>∙F<sub>1</sub>) catalyze ATP synthesis by consuming energy of electrochemical potential of hydrogen ions (<i>pmf)</i>, or ATP hydrolysis resulting in the <i>pmf</i> formation. It is generally accepted to consider F<sub>o</sub>∙F<sub>1</sub> as a reversible chemomechanical-electrical molecular machine, however: (i)&#xa0;the mechanism of energy-dependent ATP synthesis is based only on the data on hydrolytic activity of the enzyme, (ii)&#xa0;F<sub>o</sub>∙F<sub>1</sub>&#xa0;from a number of organisms effectively synthesize, but is unable to hydrolyze ATP, which indicates non-observance of the principle of microreversibility and requires development of a new hypotheses concerning the enzyme mechanism. Since 1980, the group of A.&#xa0;D.&#xa0;Vinogradov has been developing a concept according to which the elementary catalysis stages of ATP hydrolysis and ATP synthesis do not coincide, and there are two independently operating forms of F<sub>o</sub>∙F<sub>1</sub> in the coupled membranes&#xa0;– <i>pmf</i>-generating ATPase and <i>pmf</i>-consuming ATP synthase. F<sub>o</sub>∙F<sub>1</sub> of <i>P.&#xa0;denitrificans</i> as a natural model of an irreversibly functioning enzyme is a convenient object for experimental verification of the hypothesis of unidirectional energy conversion. The review considers modern concepts of the molecular mechanisms of regulation of F<sub>o</sub>∙F<sub>1</sub> ATP synthase/ATPase of <i>P.&#xa0;denitrificans</i> and development of the hypothesis of two forms of F<sub>o</sub>∙F<sub>1</sub>.</p>

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Fo∙F1 ATP-synthase/ATPase of Paracoccus denitrificans: Mystery of Unidirectional Catalysis

  • Tatiana V. Zharova,
  • Vera G. Grivennikova

摘要

Abstract

Fo∙F1 ATP synthases/ATPases (Fo∙F1) catalyze ATP synthesis by consuming energy of electrochemical potential of hydrogen ions (pmf), or ATP hydrolysis resulting in the pmf formation. It is generally accepted to consider Fo∙F1 as a reversible chemomechanical-electrical molecular machine, however: (i) the mechanism of energy-dependent ATP synthesis is based only on the data on hydrolytic activity of the enzyme, (ii) Fo∙F1 from a number of organisms effectively synthesize, but is unable to hydrolyze ATP, which indicates non-observance of the principle of microreversibility and requires development of a new hypotheses concerning the enzyme mechanism. Since 1980, the group of A. D. Vinogradov has been developing a concept according to which the elementary catalysis stages of ATP hydrolysis and ATP synthesis do not coincide, and there are two independently operating forms of Fo∙F1 in the coupled membranes – pmf-generating ATPase and pmf-consuming ATP synthase. Fo∙F1 of P. denitrificans as a natural model of an irreversibly functioning enzyme is a convenient object for experimental verification of the hypothesis of unidirectional energy conversion. The review considers modern concepts of the molecular mechanisms of regulation of Fo∙F1 ATP synthase/ATPase of P. denitrificans and development of the hypothesis of two forms of Fo∙F1.