The interaction of benzhydroxamic acid with horseradish peroxidase and its fluorescent analogs

Irit Aviram*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

Abstract

Horseradish peroxidase (HRP) reconstituted with protoporphyrin IX or zinc protoporphyrin IX binds benzhydroxamic acid with affinities of 1.54 × 104 and 8 × 102 m-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.

Original languageEnglish
Pages (from-to)483-490
Number of pages8
JournalArchives of Biochemistry and Biophysics
Volume212
Issue number2
DOIs
StatePublished - Dec 1981

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