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- W2057638514 abstract "Previous research on the mechanism of reduction of sulfate to sulfite did not establish whether the resultant sulfite is a free anion or a bound intermediate. In the present work, it has been found that the reaction product formed from 3′-phosphoryl-5′-adenosinephospho[35S]sulfate and an hydrogen donor by a yeast sulfate reductase enzyme system is a bound intermediate that is non-dialyzable and of low electrophoretic mobility. This “bound sulfite” will liberate inorganic [35S]sulfite to a disulfide acceptor to form an S-sulfonyl derivative. Partially purified “bound sulfite” will yield sulfite and sulfide in the presence of NADPH and a yeast enzyme system indicating that it is an intermediate in the enzymatic reduction of sulfate to sulfide. Methods for the partial purification of this intermediate and studies on its stability are described." @default.
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- W2057638514 date "1967-03-01" @default.
- W2057638514 modified "2023-10-12" @default.
- W2057638514 title "Yeast sulfate-reducing system III. An intermediate in the reduction of 3′-phosphoryl-5′-adenosinephosphosulfate to sulfite" @default.
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- W2057638514 doi "https://doi.org/10.1016/0304-4165(67)90074-8" @default.
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