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Fragment molecular orbital investigation of the role of AMP protonation in firefly luciferase pH-sensitivity

Authors: Bruce F. Milne, M.A.L. Marques, and Fernando Nogueira

Ref.: Phys. Chem. Chem. Phys. 12, 14285-14293 (2010)

Abstract: Firefly bioluminescence displays a sensitivity to pH changes through an alteration of the energy of the emitted photon leading to yellow-green light above ~pH 6.5 and red light below this value. Calculations using the fragment molecular orbital method have been performed on the active site of the luciferase enzyme from the Japanese firefly Luciola cruciata in order to investigate both the importance of different protonation states and tautomeric forms of the lumophore, oxyluciferin, and the role played by protonation of the active site AMP molecule. The results suggest that a single oxyluciferin species (the enol-phenolate) may be responsible for both emission colours, with changes in polarization by the active site caused by protonation of H247 as the source of the pH-dependent shift. This is reminiscent of several previously proposed models of pH-sensitivity in firefly bioluminescence and supports a recent experimental study which favoured phenolate-enol-OxyLH- as the emitter species.

Citations: 43 (Google scholar)

DOI: 10.1039/C0CP00932F

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Bibtex:

@article{Milne_2010,
	doi = {10.1039/c0cp00932f},
	url = {https://doi.org/10.1039%2Fc0cp00932f},
	year = 2010,
	publisher = {Royal Society of Chemistry ({RSC})},
	volume = {12},
	number = {42},
	pages = {14285},
	author = {Bruce F. Milne and Miguel A. L. Marques and Fernando Nogueira},
	title = {Fragment molecular orbital investigation of the role of {AMP} protonation in firefly luciferase {pH}-sensitivity},
	journal = {Physical Chemistry Chemical Physics}
}