A Thermodynamic Explanation for the Kinetic Differences Observed Using Different Chain Length Aldehydes in the in Vitro Bacterial Bioluminescent Reaction

Becvar, James E.; Wu, Li-Huey

doi:10.1016/b978-0-12-208820-9.50024-0

Cited by 1 publication

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“…The deviation of bioluminescence decay from first-order kinetics has been noted previously (Becvar and Wu, 1981;Lee and Murphy, 1975;Matheson and Lee, 1983;Shannon et al, 1978). The complex triphasic bioluminescence decay kinetics observed by Matheson and Lee (1983) at 2°C in the presence of tetradecanal as the substrate is interpreted in terms of an energy transfer scheme, where the decomposition of two distinct chemically energized species causes electronic excitation of either of two different fluorescent molecules which function as light emitters.…”

Section: Discussionsupporting

confidence: 60%

Bioluminescence decay kinetics in the reaction of bacterial luciferase with different aldehydes

Ismailov

Sobolev

Danilov

1990

J. Biolumin. Chemilumin.

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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.

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