The Modeling of Viscous Microenvironment for the Coupled Enzyme System of Bioluminescence Bacteria
Commenced in January 2007
Frequency: Monthly
Edition: International
Paper Count: 32797
The Modeling of Viscous Microenvironment for the Coupled Enzyme System of Bioluminescence Bacteria

Authors: Irina E. Sukovataya, Oleg S. Sutormin, Valentina A. Kratasyuk

Abstract:

Effect of viscosity of media on kinetic parameters of the coupled enzyme system NADH:FMN-oxidoreductase–luciferase was investigated with addition of organic solvents (glycerol and sucrose), because bioluminescent enzyme systems based on bacterial luciferases offer a unique and general tool for analysis of the many analytes and enzymes in the environment, research and clinical laboratories and other fields. The possibility of stabilization and increase of activity of the coupled enzyme system NADH:FMN-oxidoreductase–luciferase activity in vicious aqueous-organic mixtures have been shown.

Keywords: The coupled enzyme system of bioluminescence bacteria NAD(P)H:FMN-oxidoreductase–luciferase, glycerol, stabilization of enzymes, sucrose.

Digital Object Identifier (DOI): doi.org/10.5281/zenodo.1089215

Procedia APA BibTeX Chicago EndNote Harvard JSON MLA RIS XML ISO 690 PDF Downloads 1590

References:


[1] T. Baldwin, M. Nicoli, J. Becvar, and J. Hastings, "Bacterial luciferase: binding of oxidized flavin mononucleotide”, J. Biol. Chem., 250, 2763-2768, 1975.
[2] J. Hastings, C. Potrikus, S. Gupta, M. Kurfurst, and J.Makemson, "Biochemistry and physiology of bioluminescent bacteria”, Advan. Microb. Physiol., 26: 235-291, 1985.
[3] L. Lin, R. Szittner, and E. Meighen, "Binding of flavin and aldehyde to the active site of bacterial luciferase”, Bioluminescence & Chemiluminescence: Progress & Current Application, Stanley P, Kricka L., 89-92, World Scientific, Singapore, 2002.
[4] Q. Gibson, and J. Hastings, "The oxidation of reduced flavin mononucleotide by molecular oxygen” Biochem. J., 83; 368-376, 1962.
[5] A.J. Fisher, T.B. Thompson, J.B. Thoden, T.O. Baldwin, and I. Rayment, "The 1.5 Å resolution crystal structure of bacterial luciferase in low salt conditions”, J. Biol. Chem., 271, 21956-21968, 1996.
[6] V.V. Mozhaev, Y.L. Khmelnitsky, M.V. Sergeeva, N.L. Belova, N.L. Klyachko, A.V. Levashov, and K. Martinek, "Catalytic activity and denaturation of enzymes in water/organic cosolvent mixtures: a-chymotrypsin and laccase in mixed water/alcohol; water/glycol and water/formamide solvents”, Eur. J. Biochem., 184, 597– 602, 1989.
[7] M.N. Gupta, "Enzyme function in organic solvents”, Eur. J. Biochem., 203, 25-32, 1992;
[8] A.M. Klibanov, "Enzymatic catalysis in anhydrous organic solvents”, TIBS, 14, 141-189, 1989.
[9] Yu.L. Khmelnitsky, V.V. Mozhaev, N.L. Belova, M.V. Sergeeva, and K. Martinek, "Denaturation capacity: a new quntitative criterion for selection of organic sovents as reaction media in biocatalysis”, Eur. J. Biochem., 198, 31-41, 1991.
[10] A. Zaks, and A.M. Klibanov, "Enzymatic catalysis in nonaqueous solvents”, J. Biol. Chem., 263, 3194 –3201, 1988.
[11] I.E. Sukovataya, and N.A. Tyulkova, "Effect of dielectric properties of media on kinetic parameters of bioluminescent reaction”, Vestnik Moskovskogo Universiteta: Khimya, 41, 8-11, 2000.
[12] I.E. Sukovataya, and N.A. Tyulkova, "Kinetic analysis of bacterial bioluminescence in water-organic media”, Luminecsence, 16, 271-273, 2001.
[13] I.E. Sukovataya, and N.A. Tyulkova, "Effect of organic solvents on bacterial bioluminescence reaction”, Vestnik Moskovskogo Universiteta: Khimya, 44, 9-12, 2003.
[14] B.A. Illarionov, and N.A. Tyulkova, Invention Patent N 2073714 "Escherichia coli bacterial strain - producer of bacterial luciferase”, institute of Biophysics (Russian Academy of Sciences, Siberian Branch), 1997.
[15] E.V. Kudryashova, A.R. Gladilin, and A.V. Levashov, "Proteins in submolecular ensembles: research of structure by a method of resolved - time fluorescent anisotropy”, Uspekhi boil. Khimyi, 42, 257—294, 2002.