Structural basis for the spectral difference in luciferase bioluminescence

Toru Nakatsu, Susumu Ichiyama, Jun Hiratake, Adrian Saldanha, Nobuyuki Kobashi, Kanzo Sakata and Hiroaki Kato ()
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Toru Nakatsu: RIKEN Harima Institute at SPring-8
Susumu Ichiyama: RIKEN Harima Institute at SPring-8
Jun Hiratake: Kyoto University
Adrian Saldanha: Kyoto University
Nobuyuki Kobashi: RIKEN Harima Institute at SPring-8
Kanzo Sakata: Kyoto University
Hiroaki Kato: RIKEN Harima Institute at SPring-8

Nature, 2006, vol. 440, issue 7082, 372-376

Abstract: Flying Colours Fireflies communicate using coloured light that is emitted when an electronically excited oxyluciferin species — made by the enzyme luciferase — relaxes to its groundstate. Point mutants of the enzyme can dramatically alter the colour of this ‘bioluminescence’, and though the luciferase X-ray crystal structure has been solved previously, the exact nature of this colour change had eluded biologists. Nakatsu et al. have now solved the X-ray structures of luciferase in several different states, and identify a specific conformational change in an isoleucine residue as the trigger for changes in bioluminescence colour.

Date: 2006
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DOI: 10.1038/nature04542

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