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- W2024508370 abstract "Vanadyl(IV) ion enhanced markedly oxygen affinity for hemoglobin and myoglobin, but vanadate(V) did not. Optimal conditions for oxygen consumption were determined by using myoglobin and were at pH 7.7–7.9 in collidine-HC1 buffer system. Although the stoichiometry for the reaction is theoretically assumed to be one for myoglobin and four for hemoglobin depending on one electron transfer from vanadyl ion to ferric heme, the reaction ratio of vanadyl ion to myoglobin was about two, while the ratio of eight was observed in hemoglobin. Inhibition was observed in the order, EDTA>DPG>ATP, indicating that non-complexed vanadyl ion is an active form for reducing the met-heme protein. Based on these results, a possible reaction mechanism is proposed. Enhancement of oxygen binding to heme protein by vanadyl ion may be a potent biological role of the ion." @default.
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- W2024508370 date "1982-08-01" @default.
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- W2024508370 title "Vanadyl(IV) ion dependent enhancement of oxygen binding to hemoglobin and myoglobin" @default.
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- W2024508370 doi "https://doi.org/10.1016/s0006-291x(82)80146-0" @default.
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