Bioluminescence decay kinetics in the reaction of bacterial luciferase with different aldehydes.
At 22 degrees C the bioluminescence decay kinetics in the in vitro reaction catalysed by Vibrio harveyi luciferase in the presence of different aldehydes--nonanal, decanal, tridecanal and tetradecanal did not follow the simple exponential pattern and could be fitted to a two-exponential process. One more principal distinction from the first-order kinetics is the dependence of the parameters on aldehyde concentration. The complex bioluminescence decay kinetics are interpreted in terms of a scheme, where bacterial luciferase is able to perform multiple turnovers using different flavin species to produce light. The initial phase of the bioluminescent reaction appears to proceed mainly with fully reduced flavin as the substrate while the final one results from the involvement of flavin semiquinone in the catalytic cycle.
Ismailov
A D
AD
Department of Microbiology, Biological Faculty, M.V. Lomonosov Moscow State University, USSR.
Sobolev AYu
Danilov
V S
VS
D000447:Aldehydes; D005415:Flavins; D007700:Kinetics; D008156:Luciferases / Q000378:metabolism*; D008163:Luminescent Measurements; D013379:Substrate Specificity; D014733:Vibrio / Q000201:enzymology
D000447:Aldehydes; D005415:Flavins; D008156:Luciferases