Abstract
ACETATE is oxidized in animal tissues by cyclophorase1, a purified enzyme system that catalyses the tricarboxylic acid cycle and the associated phosphate exchange2,1,3,4. Dinitrophenols (about 10-4 M), which dissociate oxidations from phosphorylations5,6,7, completely inhibit cyclophorase8, as the coupling of oxidations and phosphorylations with oxidation of acetate, etc., seems to be essential for cyclophorase activity. Acetate oxidation by Saccharomyces cerevisiæ9,10,11, Pseudomonas calcoacetica12, and Escherichia coli13 is not apparently inhibited, or may be even increased12,9,10, by 10-4 M 2,4 dinitrophenol, which is inconsistent with the hypothesis that in the micro-organisms referred to, acetate is oxidized by a cyclophorase-like system. The whole problem, therefore, requires re-investigation, as Cross et al. have noted2, especially when the tricarboxylic acid cycle is the main pathway for acetate oxidation in yeast.
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STOPPANI, A. Effect of Dinitrophenols on Acetate Oxidation by Saccharomyces cerevisiæ. Nature 164, 1096–1097 (1949). https://doi.org/10.1038/1641096a0
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DOI: https://doi.org/10.1038/1641096a0
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