nimbus8 - 12-6-2013 at 21:47
The following reaction displays the reduction of luciferase to oxidize luciferin.
http://www.sigmaaldrich.com/content/dam/sigma-aldrich/life-s...
Many studies have showed that oxidation of luciferin in the absence of luciferase did not lead to bioluminescence. This leads me to believe that is is
the reduction of luciferase that truly causes light to be released. And in that case couldn't electrolysis of some luciferase solution cause continual
luminescence.
nimbus8 - 12-6-2013 at 21:54
Oh wow, im an idiot. Its not the luciferase thats being reduced. But still the conclusion remains that its the luciferase causing the luminescence.
Because apparently when it helps oxidize luciferol it puts oxyluciferol in a higher state than normal oxidation
But by this logic, assuming none of the luciferase is used in the reaction, you could perform electrolysis on the mixture to convert the oxyluciferin
back to luciferin and the reaction could occur indefinitely.
[Edited on 13-6-2013 by nimbus8]
Dr.Bob - 13-6-2013 at 09:06
That would be tough to do, as the CO2 eliminated in the light forming step may not just jump back onto the luciferin without some help. If you want
to produce light using electricity, I think there are better ways. I'm quite sure that there are actual papers that describe the details of
luciferin oxidation with more clear mechanisms as to what the light producing steps are, but the enzyme is making a phosphoester, which is likely a
better leaving group that a plain oxygen. A simple oxidation of the luciferin would not generate such a specific oxidation of the thiazole acid to a
phenol, that would be quite unlikely.