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Krasnova O. I., Tyulkova N. A., Doroshenko I. O., Frank L. A.

Bacterial bioluminescence with flavinmononucleotide activated by n- methylimidazole

Abstract

The substrate of bacterial luciferase – flavin mononucleotide was activated by N- methylimidazole on phosphate group. The properties of obtained derivate of the FMN and its interaction with bacterial luciferase from Photobacterium leiognathi were investigated. The activated substrate in nonreduced form modify the enzyme on the SH-group by means of increasing its reactionability, it lead to irreversible inactivation. The reduced form of activated FMN derivative possesses different properties in dependence from the method of its reduction. When the activated FMNH2 derivative is photoreduced it don’t show the luminescence in reaction with luciferase. The prolonged luminescence of low intensity is observed by using of the chemically reduced activated flavin derivative. The activated FMN derivative competes for a active site of enzyme with native FMN. The Michael’s constants and inhibition rate constants of reaction were calculated. It is assumed that differences in behavior of the activated flavin derivative are conditioned by intensification of electronegativity of phosphate group of the flavin.
Moscow University Chemistry Bulletin.
2003, Vol. 44, No. 1, P. 5
   

Copyright (C) Chemistry Dept., Moscow State University, 2002
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