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• W2019672311 abstract "Horseradish peroxidase (HRP) reconstituted with protoporphyrin IX or zinc protoporphyrin IX binds benzhydroxamic acid with affinities of 1.54 × 104 and 8 × 102m−1, respectively. This interaction is competitive with respect to hydrogen donor substrates of peroxidase. The steady-state oxidation of benzhydroxamic acid by HRP was studied by monitoring the disappearance of the hydroxamate function and the formation of nitrite. The inhibition by benzhydroxamic acid of oxidation of HRP substrates may be classified as an inhibition by a competing substrate. In the case of HRP-catalyzed oxidation of ferrocyanide a marked activating effect of benzhydroxamic acid was observed. Mechanisms responsible for this effect are discussed." @default.
• W2019672311 created "2016-06-24" @default.
• W2019672311 creator A5090357174 @default.
• W2019672311 date "1981-12-01" @default.
• W2019672311 modified "2023-09-24" @default.
• W2019672311 title "The interaction of benzhydroxamic acid with horseradish peroxidase and its fluorescent analogs" @default.
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• W2019672311 doi "https://doi.org/10.1016/0003-9861(81)90391-x" @default.
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