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- W1978889127 abstract "The stability of oxyperoxidases increased in the order meso- < proto < chlorocruoro- < diacetylperoxidases, which was an increasing order of electron-withdrawing capacities of 2,4-substituents of deuteroheme and the ratio of Δlogk1toΔpK3 was approximately 0.6 in the two series of isoenzyme preparations, horseradish peroxidases A and (B + C), where k1andpK3 represent a rate constant for conversion from an oxyperoxidase to the ferric enzyme and a measure of basicity of pyrrole nitrogen of the substituted deuterohemes, respectively. Deutero-oxyperoxidases A and (B + C) were definitely more stable than expected from the above linear relationship. The stability of peroxidase Compound I also varied with the 2,4-substituents, but it did not necessarily correlate with electron-withdrawing capacities of the substituents. Natural peroxidases formed relatively stable Compound I in both series of the isoenzymes. From these results it was concluded that the stability of oxyperoxidases was affected by the electron density at the iron atom of the enzyme while steric factors might be involved in stabilizing Compound I." @default.
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- W1978889127 date "1976-03-01" @default.
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- W1978889127 title "Effects of 2,4-Substituents of deuteroheme upon the stability of the oxy-form and compound I of horseradish peroxidases" @default.
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- W1978889127 doi "https://doi.org/10.1016/0003-9861(76)90235-6" @default.
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