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BIOLUMINESCENCE FROM THE REACTION OF FMN, H 2 O 2 AND LONG CHAIN ALDEHYDE WITH BACTERIAL LUCIFERASE
Author(s) -
Hastings J. W.,
Tu ShiaoChun,
Becvar James E.,
Presswood Robert P.
Publication year - 1979
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1979.tb07062.x
Subject(s) - bioluminescence , flavin group , luciferase , flavin mononucleotide , aldehyde , chemistry , photochemistry , chromophore , chemiluminescence , quantum yield , stereochemistry , enzyme , catalysis , biochemistry , fluorescence , organic chemistry , transfection , physics , quantum mechanics , gene
— The bioluminescent oxidation of reduced flavin mononucleotide by bacterial luciferase involves a long‐lived flavoenzyme intermediate whose chromophore has been postulated to be the 4a‐sub‐stituted peroxy anion of reduced flavin. Reaction of long chain aldehyde with this intermediate results in light emission and formation of the corresponding acid. These experiments show that the typical aldehyde‐dependent, luciferase‐catalyzed bioluminescence can also be obtained starting with FMN and H 2 O 2 instead of FMNH 2 and O 2 . We postulate that the 4a‐peroxy anion intermediate is formed directly by attack of H 2 O 2 on FMN. The latter may be bound to luciferase. An enzyme bound intermediate is formed which by kinetic analysis, flavin specificity for luminescence, aldehyde dependence, and bioluminescent emission spectrum appears to be identical with the species generated by reaction of FMNH, and O 2 with luciferase. The quantum yield of the H 2 O 2 ‐ ‐ and FMN‐initiated biolumlnescence is low but can be enhanced by certain metal ions, which also stimulate a chemiluminescent reaction of oxidized flavin with H 2 O 2 . The peak of this chemiluminescence. however, appears to be at a shorter wavelength than that (490 nm) of the bioluminescence.