Initiation and inhibition of free-radical processes in biochemical peroxide systems: A review

Autor:	D. I. Metelitsa, E. I. Karaseva
Rok vydání:	2007
Předmět:	chemistry.chemical_classification Antioxidant ABTS biology medicine.medical_treatment Applied Microbiology and Biotechnology Biochemistry Peroxide Catalysis chemistry.chemical_compound Enzyme chemistry biology.protein medicine Organic chemistry Tetrazole Phenols Peroxidase
Zdroj:	Applied Biochemistry and Microbiology. 43:481-505
ISSN:	1608-3024 0003-6838
DOI:	10.1134/s000368380705002x
Popis:	The role of complexes containing oxygen or peroxide in monooxygenase systems and models thereof, as well as in peroxidase- and quasi-peroxidase-catalyzed processes, has been reviewed. Pathways of conversion of these intermediate complexes involving single-electron (radical) and two-electron (heterolytic) mechanisms are dealt with. Coupled peroxidase-catalyzed oxidation of aromatic amines and phenols is analyzed; inhibition and activation of peroxidase-catalyzed reactions are characterized quantitatively. Oxidation of chromogenic substrates (ABTS, OPD, and TMB) in the presence of phenolic inhibitors or polydisulfides of substituted phenols is characterized by inhibition constants (Ki, micromol). Activation of peroxidase-catalyzed oxidation of the same substrates is characterized by the degree (coefficient) of activation (alpha, M(-1)), which was determined for 2-aminothiazole, melamine, tetrazole, and its 5-substituted derivatives. Examples of applied use of peroxidase-catalyzed enzyme and model systems are given (oxidation of organic compounds, chemical analysis, enzyme immunoassay, tests for antioxidant activity of biological fluids).
Databáze:	OpenAIRE
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