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NAPHTHYL‐ AND QUINOLYLLUCIFERIN: GREEN AND RED LIGHT EMITTING FIREFLY LUCIFERIN ANALOGUES
Author(s) -
BRANCHING BRUCE R.,
HAYWARD MATTHEW M.,
BAMFORD SARAH,
BRENNAN PATRICIA,
LAJINESS EVELYN J.
Publication year - 1989
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.1751-1097.1989.tb08442.x
Subject(s) - bioluminescence , chemistry , photoprotein , luciferin , luciferase , light emission , firefly protocol , photochemistry , benzothiazole , kinetics , substrate (aquarium) , moiety , fluorescence , stereochemistry , biochemistry , materials science , transfection , zoology , physics , optoelectronics , oceanography , quantum mechanics , biology , gene , geology
In the course of investigations on the possible involvement of the CIEEL (chemically initiated electron‐exchange luminescence) mechanism in firefly bioluminescence, we have synthesized two novel firefly luciferin substrate analogues. D‐Naphthylluciferin and D‐quinolylluciferin were prepared by condensing D‐cysteine with 2‐cyano‐6‐hydroxynaphthalene and 2‐cyano‐6‐hydroxyquinoline, respectively. These analogues are the first examples of bioluminescent substrates for firefly luciferase that do not contain a benzothiazole moiety. Firefly luciferase‐catalyzed bioluminescence emission spectra revealed that compared to the normal yellow‐green light of luciferin (γ max = 559 nm), the emission from naphthylluciferin is significantly blue‐shifted (γ max = 524 nm); whereas quinolylluciferin emits orange‐red light (γ max = 608 nm). The fluorescence emission spectra, reaction pH optima, relative light yields, light emission kinetics and K M values of the analogues also were measured and compared to those of luciferin. Neither of the analogues produced the characteristic flash kinetics observed for the natural substrate. Instead, slower rise times to peak emission intensity were recorded. It appears that the formation of an intermediate from the analogue adenylates prior to the addition of oxygen is responsible for the slow rise times. The synthetic substrate analogues described here should be useful for future mechanistic studies.