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