THE INTERACTION OF BENZHYDROXAMIC ACID WITH HORSERADISH-PEROXIDASE AND ITS FLUORESCENT ANALOGS

被引:36
作者
AVIRAM, I
机构
关键词
D O I
10.1016/0003-9861(81)90391-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Horseradish peroxidase (HRP) reconstituted with protoporphyrin IX or zinc protoporphyrin IX binds benzhydroxamic acid with affinities of 1.54 .times. 104 and 8 .times. 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 each of HRP-catalyzed oxidation of ferrocyanide a marked activating effect of benzhydroxamic acid was observed. Mechanisms responsible for this effect are discussed.
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页码:483 / 490
页数:8
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