The Chemistry of Light Emission

McElroy, W. D.; Seliger, H. H.

doi:10.1002/9780470122709.ch3

Cited by 23 publications

(4 citation statements)

References 119 publications

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“…Although the experimental evidence is scarce [26], or even nonexistent [27], oxyluciferin (referred to as ‘the product’) is frequently referred as the compound that causes the inhibition that induces the premature light decay [7,14,28–30]. The allosteric mechanism proposed by Ford et al .…”

Section: Resultsmentioning

confidence: 99%

Coenzyme A affects firefly luciferase luminescence because it acts as a substrate and not as an allosteric effector

et al. 2005

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The effect of CoA on the characteristic light decay of the firefly luciferase catalysed bioluminescence reaction was studied. At least part of the light decay is due to the luciferase catalysed formation of dehydroluciferyl‐adenylate (L‐AMP), a by‐product that results from oxidation of luciferyl‐adenylate (LH2‐AMP), and is a powerful inhibitor of the bioluminescence reaction (IC50 = 6 nm). We have shown that the CoA induced stabilization of light emission does not result from an allosteric effect but is due to the thiolytic reaction between CoA and L‐AMP, which gives rise to dehydroluciferyl‐CoA (L‐CoA), a much less powerful inhibitor (IC50 = 5 µm). Moreover, the Vmax for L‐CoA formation was determined as 160 min−1, which is one order of magnitude higher than the Vmax of the bioluminescence reaction. Results obtained with CoA analogues also support the thiolytic reaction mechanism: CoA analogues without the thiol group (dethio‐CoA and acetyl‐CoA) do not react with L‐AMP and do not antagonize its inhibitor effect; CoA and dephospho‐CoA have free thiol groups, both react with L‐AMP and both antagonize its effect. In the case of dephospho‐CoA, it was shown that it reacts with L‐AMP forming dehydroluciferyl‐dephospho‐CoA. Its slower reactivity towards L‐AMP explains its lower potency as antagonist of the inhibitory effect of L‐AMP on the light reaction. Moreover, our results support the conjecture that, in the bioluminescence reaction, the fraction of LH2‐AMP that is oxidized into L‐AMP, relative to other inhibitory products or intermediates, increases when the concentrations of the substrates ATP and luciferin increases.

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Section: Resultsmentioning

confidence: 99%

Coenzyme A affects firefly luciferase luminescence because it acts as a substrate and not as an allosteric effector

et al. 2005

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“…[21][22][23][60][61][62] Ultraweak chemiluminescence was soon related to the direct utilization of molecular oxygen and the production of electronically excited states in biologic systems. 18,19,[21][22][23]62 Many comparative studies on different assays have been completed by utilizing UPE, compared to other assays. One line focused on doxorubicin-induced lipid peroxidation, which is generally evaluated by 2-thiobarbituric acid reactive substance formation.…”

Section: Discussionmentioning

confidence: 99%

“…17 In the present study, attention is drawn to the method of recording ultraweak photon emission (UPE) to detect electronically excited states in complex biologic systems. UPE is related to the direct utilization of molecular oxygen 18,19 and the production of electronically excited states in biologic systems, 20 in particular, the oxygen-dependent chain reactions involving biologic lipids. [21][22][23] Chemiluminescence was already utilized in the late 1970s and 1980s to monitor enzymatic reactions and biochemical processes involving free radicals in organ systems, [24][25][26][27][28] blood, [28][29][30][31][32] and subcellular fractions.…”

Section: Introductionmentioning

confidence: 99%

Differential Effects of Relaxation Techniques on Ultraweak Photon Emission

Wijk¹,

Lüdtke

Wijk

2008

The Journal of Alternative and Complementary Medicine

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“…The energy associated to the emission of a mole of yellow-green photons, as in Photinus pyralis, was far superior to that corresponding to the hydrolysis of ATP. 11 The conditions that influenced the bioluminescence reaction, namely temperature and pH, were studied but the interpretation of those results was limited, as McElroy acknowledged, 12 by the purity of the substrates and enzyme used. Nonetheless, the bioluminescence was found to be dependent on four components: oxygen, the enzyme, the substrate luciferin (LH 2 ) and ATP•Mg 2+ .…”

Section: First Studies and Luciferin Adenylationmentioning

confidence: 99%