2. Biochemical mechanism of bacterial bioluminescence
The reaction of bacterial luminescence is catalyzed by luciferase, an enzyme composed of two subunits, called α and β (Belas et al. 1982). The luciferase substrates are long-chain aldehydes and FMNH2. The reaction leads to the oxidation of FMNH2 to FMN and the oxidation of the aldehydes to organic (fatty) acids. A quantum of light is an additional product of this reaction, which can be summarized as follows:
RCHO + FMNH2 + O2 → RCOOH + FMN+H2O + hν
The fatty acids produced in the reaction catalyzed by luciferase are subsequently reduced to aldehydes by a specific reductase. In the same reaction, NADPH + H+ is converted to NADP+ and ATP is hydrolyzed to ADP (Ziegler & Baldwin 1981). FMNH2, which is necessary for the luminescence reaction (see above), is generated from FMN by NAD(P)H–FMN oxidoreductase (Jabłoński & DeLuca 1978).
As can be deduced from the above description, bioluminescence is an energy-consuming reaction. In fact, for light emission bacteria may use up to 20% of the total cellular energy (Nealson & Hastings 1979, Bassler & Silverman 1995).