1955
DOI: 10.1016/0006-3002(55)90014-7
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Sulphite oxidation by a plant mitochondrial system

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Cited by 30 publications
(4 citation statements)
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“…All the evidence available indicates that sulfite is an intermediate in the oxidation of thiosulfate (and other reduced sulfur compounds) and is oxidized to sulfate by a phosphorylative pathway rather than by the sulfite oxidase described in mammalian tissue. An effect of AMP on the oxidation of sulfite was observed previously in plants, but neither phosphorylation or APS formation was reported (123). Although sulfite can be produced from the reductive cleavage of thiosulfate, it is possible that sulfite can be formed by other mechanisms, namely, the postulated polythionate cycle (65).…”
Section: ] 83mentioning
confidence: 85%
“…All the evidence available indicates that sulfite is an intermediate in the oxidation of thiosulfate (and other reduced sulfur compounds) and is oxidized to sulfate by a phosphorylative pathway rather than by the sulfite oxidase described in mammalian tissue. An effect of AMP on the oxidation of sulfite was observed previously in plants, but neither phosphorylation or APS formation was reported (123). Although sulfite can be produced from the reductive cleavage of thiosulfate, it is possible that sulfite can be formed by other mechanisms, namely, the postulated polythionate cycle (65).…”
Section: ] 83mentioning
confidence: 85%
“…Undoubtedly, part of the sulfite is directly oxidized according to the redox conditions prevailing in the cell. A sulfite oxidase was found in plant mitochondria (TAGER and RAUTANEN 1955). It needs Mg++ and cytochrome c for activity, but we do not know to which extent it participates in sulfite oxidation in the leaf.…”
Section: C) Sulfite Metabolism and Transportmentioning
confidence: 96%
“…The quantitative nature of the activation of amino acid decarboxylations by AMP-5' is comparable with other enzymes recently found to be activated by this nucleotide. For example, Tager & Rautanen (1955) found that the degree of stimulation by AMP-5' of sulphite oxidation in oat mitochondria was a function of the AMP-5' concentration. Madsen & Cori (1955) found that muscle phosphorylase a binds 4 moles of AMP-5'/mole of protein and phosphorylase b binds 2 moles of AMP-5'/mole of protein, and that whereas the b enzyme has an absolute requirement for AMP-5', the a enzyme is still 65 % active in its absence.…”
Section: Activation Of Amino Acid Decarboxylasesmentioning
confidence: 99%