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Maier, K.L. ; Hinze, H. ; Leuschel, L.

Mechanism of sulfite action on the energy metabolism of Saccharomyces cerevisiae.

Biochim. Biophys. Acta-Bioenerg. 848, 120-130 (1986)

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Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.

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The pools of ribonucleoside di- and triphosphates decrease within a few min after addition of 5 mM sulfite to a suspension of Saccharomyces cerevisiae at pH 3.6. Levels of the corresponding ribonucleoside monophosphates increase in parallel. The strongest effect was observed with the adenosine phosphate pools. Depletion of ATP by sulfite at pH 3.6 occurs both in the presence and absence of glucose. These findings point to at least two different mechanisms for sulfite action on energy metabolism. Glycolysis is effectively impaired by low sulfite concentrations. The enzymes glyceraldehyde-3-phosphate dehydrogenase and alcohol dehydrogenase are inhibited by sulfite in vitro. In addition, formation of adducts between sulfite and aldehydes contributes to the inhibition of enzymatic reactions as shown with alcohol dehydrogenase. Sulfite also causes reduction of oxygen consumption of glucose-starved yeast at pH 3.6 which coincides with ATP depletion. In vitro, the oligomycin-sensitive F1-ATPase of yeast is stimulated 2.8-fold by 1 mM sulfite at pH 5.7. However, this stimulation does not seem to be involved in sulfite-initiated ATP depletion as concluded from experiments with the F1-ATPase-deficient mutant pet 936. At pH 3.6, the intracellular proton concentration of yeast is increased from 3.2-6.3·10-8 M to 4.0·10-6 M by 1 mM sulfite. In spite of the marked intracellular acidification, stimulation of an ATP-driven proton pump is not the chief cause for the sulfite-initiated ATP decrease. During short exposure of yeast to sulfite the effect on energy metabolism is reversible.

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