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Hinze, H. ; Holzer, H.

Analysis of the energy metabolism after incubation of Saccharomyces cerevisiae with sulfite or nitrite.

Arch. Microbiol. 145, 27-31 (1986)
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After addition of 5 mM sulfite or nitrite to glucose-metabolizing cells of Saccharomyces cerevisiae a rapid decrease of the ATP content and an inversely proportional increase in the level of inorganic phosphate was observed. The concentration of ADP shows only small and transient changes. Cells of the yeast mutant pet 936, lacking mitochondrial F1ATPase, after addition of 5 mM sulfite or nitrite exhibit changes in ATP, ADP and inorganic phosphate very similar to those observed in wild type cells. They key enzyme of glucose degradation, glyceraldehyde-3-phosphate dehydrogenase was previously shown to be the most sulfiteor nitrite-sensitive enzyme of the glycolytic pathway. This enzyme shows the same sensitivity to sulfite or nitrite in cells of the mutant pet 936 as in wild type cells. It is concluded that the effects of sulfite or nitrite on ATP, ADP and inorganic phosphate are the result of inhibition of glyceraldehyde-3-phosphate dehydrogenase and not of inhibition of phosphorylation processes in the mitochondria. Levels of GTP, UTP and CTP show parallel changes to ATP. This is explained by the presence of very active nucleoside monophosphate kinases which cause a rapid exchange between the nucleoside phosphates. The effects of the sudden inhibition of glucose degradation by sulfite or nitrite on levels of ATP, ADP and inorganic phosphate are discussed in terms of the theory of Lynen (1942) on compensating phosphorylation and dephosphorylation in steady state glucose metabolizing yeast.
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords Nitrite; Sulfite; Saccharomyces cerevisiae; ATP; Energy metabolism; Inorganic phosphate; Glyceraldehyde-3-phosphate dehydrogenase; Glucose-6-phosphate dehydrogenase
ISSN (print) / ISBN 0003-9276
e-ISSN 1432-072X
Journal Archives of Microbiology
Quellenangaben Volume: 145, Issue: 1, Pages: 27-31 Article Number: , Supplement: ,
Publisher Springer
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Abteilung für Enzymchemie