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Effect of quinones and phenols on the triple‐enzyme bioluminescent system with protease
Author(s) -
Kudryasheva N. S.,
Esimbekova E. N.,
Remmel N. N.,
Kratasyuk V. A.,
Visser A. J. W. G.,
van Hoek A.
Publication year - 2003
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.731
Subject(s) - chemistry , trypsin , phenols , bioluminescence , enzyme , protease , redox , fluorescence , stereochemistry , biochemistry , photochemistry , organic chemistry , physics , quantum mechanics
Abstract The study addressed the effects of redox‐active compounds on trypsin activity. Series of organic oxidizers (quinones) and reducers (phenols) were chosen as model redox‐active compounds. Trypsin activity was quantied by bioluminescent technique. Interactions of these compounds with trypsin were studied by uorescent and light absorption methods. Luminescence intensity decay constants in the reduced nicotinamidadeninedinucleotide (NADH): avinmononucleotide (FMN)‐oxidoreductase (R)–luciferase (L)–trypsin (T) (R + L + T) triple‐enzyme system were calculated and compared in the presence of different concentrations of quinones and phenols. The triple‐enzyme system was shown to be sensitive to quinones and not sensitive to phenols. It has been found that the effects produced by quinones on the coupled enzyme system (R + L) and on the trypsin molecule (T) are not related. The conclusions were extrapolated to the properties of other proteases and antiproteases. Copyright © 2003 John Wiley & Sons, Ltd.