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. 2008 Sep 27;14(3):195–203. doi: 10.1007/s12298-008-0019-x

ATP synthesis catalyzed by a V-ATPase: an alternative pathway for energy conservation operating in plant vacuoles?

Arnoldo Rocha Façanha 1,✉, Anna Lvovna Okorokova-Façanha 2,3
PMCID: PMC3550615  PMID: 23572887

Abstract

The electrochemical H+ gradient generated in tonoplast vesicles isolated from maize seeds was found to be able to drive the reversal of the catalytic cycle of both vacuolar H+-pumps (Façanha and de Meis, 1998). Here we describe the reversibility of the vacuolar V-type H+-ATPase (V-ATPase) even in the absence of the H+ gradient in a water-Me2SO co-solvent mixture, resulting in net synthesis of [γ-32P]ATP from [32P]Pi and ADP. The water-Me2SO (5 to 20 %) media promoted inhibition of both PPi hydrolysis and synthesis reactions whereas it slightly affected the ATP hydrolysis and clearly stimulated the ATP synthesis, which was unaffected by uncoupling agents (FCCP, Triton X-100 or NH4+). This effect of Me2SO on the ATP⇔32P exchange reaction seems to be related to a decrease of the apparent Km of the V-ATPase for Pi. The results are in accordance to the concept that the energetics of ATP synthesis catalysis depends on the solvation energies interacting in the enzyme microenvironment. A possible physiological significance of this phenomenon for the metabolism of desiccation-tolerant plant cells is discussed.

Key words: bind energy, proton pumps, proton gradient, DMSO, corn seeds, V1V0-ATPase, membrane bound H+-pyrophosphatase

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Abbreviations

ACMA

9-amino-6-chloro-2-methoxyacridine

FCCP

carbonyl cyanide p(trifluoromethoxy)-phenylhydrazone

Me2SO

dimethyl sulfoxide

V-ATPase

V-type H+-ATPase

H+-PPase

membrane-bound H+ pyrophosphatase

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