Spectroscopic evidence that salicylic acid converts a temporally inactivated form of horseradish peroxidase (compound III) to the irreversibly inactivated verdohemoprotein (P-670).
نویسندگان
چکیده
We obtained spectroscopic evidence in support of salicylate-dependent inactivation of horseradish peroxidase-C. Addition of salicylate to the enzyme arrested at a temporal inactive state (Compound III) in the presence of H2O2, resulted in rapid and irreversible inactivation of the enzyme yielding verdohemoproteins (P-670). Multiple roles for salicylate in peroxidase-catalyzed reactions are discussed.
منابع مشابه
Spectroscopic evidence in support of horseradish peroxidase compound II-catalyzed oxidation of salicylic acid but not of phenylethylamine.
Salicylic acid and phenylethylamine are putative substrates for naturally occurring reactions for generation of reactive oxygen species, which are catalyzed by plant peroxidases. Here, we used commercially available highly purified horseradish peroxidase-C (HRP-C) as a model enzyme for spectroscopic analysis, and obtained data suggesting that the Compound II form of HRP-C does not utilize pheny...
متن کاملThe conversion of horseradish peroxidase C to a verdohemoprotein by a hydroperoxide derived enzymatically from indole-3-acetic acid and by m-nitroperoxybenzoic acid.
A verdohemoprotein was formed from Compound I of horseradish peroxidase C upon the addition of about 2 molar equivalents of m-nitroperoxybenzoic acid (mNPBA) or hydroperoxide formed from indole-3-acetic acid during its catalytic oxidation. The formation of the verdohemoprotein occurred via two intermediates which have an absorbance peak at 965 or 940 nm. Carbon monoxide was evolved in the react...
متن کاملELUCIDATION OF pK VALUES FOR ACTIVE SITE OF HORSERADISH PEROXIDASE AND BINDING STUDY OF INTERACTION WITH N-PHENYL BENZHYDROXAMIC ACID USING A SPECIAL DIFFERENCE SPECTROPHOTOMETRIC TECHNIQUE
The binding behavior of a competitive inhibitor, N-phenylbenzhydroxamic acid (BHA) against horseradish peroxidase (HRP) was studied in order to understand and predict the interaction mechanism of hydrogen donors with the enzyme. The dissociation constants of the complexes of HRP-BHA, HRP-donor and HRP-BHA-azide were estimated at specified conditions by difference spectroscopy. The binding s...
متن کاملOxidation of melatonin and tryptophan by an HRP cycle involving compound III.
We recently described that horseradish peroxidase (HRP) and myeloperoxidase (MPO) catalyze the oxidation of melatonin, forming the respective indole ring-opening product N(1)-acetyl-N(2)-formyl-5-methoxykynuramine (AFMK) (Biochem. Biophys. Res. Commun. 279, 657-662, 2001). Although the classic peroxidatic enzyme cycle is expected to participate in the oxidation of melatonin, the requirement of ...
متن کاملCobalt-substituted horseradish peroxidase.
Horseradish peroxidase can be reconstituted with cobalt porphyrin to give a cobaltic holoenzyme having physicochemical properties quite similar to those of the native ferric protein. The cobaltic protein (Co3+HRP) can be reduced to the cobaltous form (CoHRP), the analogue of ferroperoxidase and the reduced cobalt protein can bind O2 to form an analogue of oxyferroperoxidase (Compound III). Sinc...
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ورودعنوان ژورنال:
- Bioscience, biotechnology, and biochemistry
دوره 66 3 شماره
صفحات -
تاریخ انتشار 2002