INTERACTION OF PHOTOBACTERIUM-LEIOGNATHI AND VIBRIO-FISCHERI Y1 LUCIFERASES WITH FLUORESCENT (ANTENNA) PROTEINS - BIOLUMINESCENCE EFFECTS OF THE ALIPHATIC ADDITIVE
Vn. Petushkov et al., INTERACTION OF PHOTOBACTERIUM-LEIOGNATHI AND VIBRIO-FISCHERI Y1 LUCIFERASES WITH FLUORESCENT (ANTENNA) PROTEINS - BIOLUMINESCENCE EFFECTS OF THE ALIPHATIC ADDITIVE, Biochemistry, 35(37), 1996, pp. 12086-12093
The kinetics of the bacterial bioluminescence reaction is altered in t
he presence of the fluorescent (antenna) proteins, lumazine protein (L
umP) from Photobacterium or the yellow fluorescence proteins (YFP) hav
ing FMN or Rf bound, from Vibrio fischeri strain Y1, Depending on reac
tion conditions, the bioluminescence intensity and its decay rate may
be either enhanced or strongly quenched in the presence of the fluores
cent proteins. These effects call be simply explained on the basis of
the same protein-protein complex model that accounts for the biolumine
scence spectral shifts induced by these fluorescent proteins. In such
a complex, when the fluorophore evidently is in proximity to the lucif
erase active site, it is expected that the on-off rate of certain alip
hatic components of the reaction should be altered with a consequent s
hift in the equilibria among the luciferase intermediates, as recently
elaborated in a kinetic scheme, These aliphatic components are the bi
oluminescence reaction substrate, tetradecanal or other long-chain ald
ehyde, its carboxylic acid product, or dodecanol used as a stabilizer
of the luciferase peroxyflavin. No evidence can be found or the protei
n-protein interaction in the absence of the aliphatic component.