Bacterial luciferase. Binding of oxidized flavin mononucleotide.
نویسندگان
چکیده
منابع مشابه
Interaction of bacterial luciferase with 8-substituted flavin mononucleotide derivatives.
Bacterial luciferase catalyzes the emission of visible light from the reaction of reduced flavin, molecular oxygen, and an n-alkyl aldehyde. The mechanism of the reaction was probed by measuring the electronic effects of various substituents at the 8-position of the flavin ring system. Substituent effects were obtained for CH3-, Cl-, CH3O-, CH3S-, F-, and H- on the rate of formation and decay o...
متن کاملBioluminescence emission from the reaction of luciferase-flavin mononucleotide radical with O2-..
The blue neutral luciferase flavin radical has been shown not to be in a catalytically significant equilibrium with species leading to emission of light [Kurfürst, M., Ghisla, S., Presswood, R., & Hastings, J. W. (1982) Eur. J. Biochem. 123, 355-361]. It is shown here that this radical can nevertheless react with O2-. to form a species that is competent in light emission. From its properties, t...
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The protein (AfpA, for archaeoflavoprotein) encoded by AF1518 in the genome of Archaeoglobus fulgidus was produced in Escherichia coli and characterized. AfpA was found to be a homodimer with a native molecular mass of 43 kDa and containing two noncovalently bound flavin mononucleotides (FMNs). The cell extract of A. fulgidus catalyzed the CO-dependent reduction of AfpA that was stimulated by t...
متن کاملStudies on the binding and function of flavin phosphates with flavin mononucleotide-dependent enzymes.
The binding and function of FMN, 3,6,7-trimethyl-9(l’-o-ribityl)isoahoxazine 5’-phosphate (3-methyl-FMN), 6,7dichloro-9-(l’-o-ribityl)isoalloxazine 5’-phosphate (6,7-dichloro-FMN), and 6,7-dimethyl-9-(5’-hydroxypentyl)isoalloxazine 5’-phosphate (5’-hydroxypentyl-FMN) has been investigated with reduced nicotinamide adenine dinucleotide phosphate dehydrogenase and NADPH cytochrome c reductase fro...
متن کاملIsolation and characterization of the transient, luciferase-bound flavin-4a-hydroxide in the bacterial luciferase reaction
Procedures and conditions have been established such that the unstable enzyme-bound flavin intermediate produced in the bacterial luciferase reacti~ can be isolated as approximately 70% of the flavin product, the remaining being the final product, FMN. The structure of the intermediate is proposed to be that of a luciferase-bound 4a,5-dihydroflavin-4a-hydroxide. The intermediate has a half-life...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1975
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)41555-x