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Structure and Catalytic Inactivity of the Bacterial Luciferase Neutral Flavin Radical.
- Source :
-
European Journal of Biochemistry . 4/1/82, Vol. 123 Issue 2, p355-361. 7p. - Publication Year :
- 1982
-
Abstract
- A luciferase-bound neutral flavin semiquinone radical can be formed upon the oxidation of the luciferase- FMNH2 complex by molecular oxygen. This species can also be formed anaerobically by comproportionation of FMN and FMNH2 in the presence of luciferase. The radical is kinetically stable (t1/2 ≈ 20 h at 0 °C in air: the Arrhenius ΔHdecay= being about 170 kJ/mol) and can be prepared in pure form by Sephadex G-25 chromatography at 0-4 C. The pure enzyme-bound radical is inactive for light emission either with or without aldehyde, and is not in (relevantly rapid) equilibrium with the luciferase 4a-peroxyflavin, the active intermediate in the bioluminescent reaction. [ABSTRACT FROM AUTHOR]
- Subjects :
- *FLAVINS
*BACTERIA
*COENZYMES
*FLAVOPROTEINS
*ENZYMES
*COLLOIDS
Subjects
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 123
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 15803545
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1982.tb19775.x