Intermediates bacterial bioluminescence

Fig. 2.1 Mechanism of the bacterial bioluminescence reaction. The molecule of FMNH2 is deprotonated at N1 when bound to a luciferase molecule, which is then readily peroxidized at C4a to form Intermediate A. Intermediate A reacts with a fatty aldehyde (such as dodecanal and tetradecanal) to form Intermediate B. Intermediate B decomposes and yields the excited state of 4a-hydroxyflavin (Intermediate C) and a fatty acid. Light (Amax 490 nm) is emitted when the excited state of C falls to the ground state. The ground state C decomposes into FMN plus H2O. All the intermediates (A, B, and C) are luciferase-bound forms. The FMN formed can be reduced to FMNH2 in the presence of FMN reductase and NADH.

Eckstein, J. W., Hastings, J. W., and Ghisla, S. (1993). Mechanism of bacterial bioluminescence. 4a,5-Dihydroflavin analogs as models for luciferase hydroperoxide intermediates and the effect of substituents at the 8-position of flavin on luciferase kinetics. Biochemistry 32 404 111. 

Lee, J., Wang, Y., and Gibson, B. G. (1991a). Electronic excitation transfer in the complex of lumazine protein with bacterial bioluminescence intermediates. Biochemistry 30 6825-6835. 

Raushel, F. M., and Baldwin, T. O. (1989). Proposed mechanism for the bacterial bioluminescence reaction involving dioxirane intermediate. Biochem. Biophys. Res. Commun. 164 1137-1142. 

Wada, N., etal. (1997). A theoretical approach to elucidate a mechanism of O2 addition to intermediate I in bacterial bioluminescence. In Hastings, J. W., etal. (eds.), Biolumin. Chemilumin., Proc. Int. Symp., 9th, 1996, pp. 58-61. Wiley, Chichester, UK. 

Meighen E, Mac-Kenzie R, Flavin specificity of enzyme-substrate intermediates in the bacterial bioluminescent reaction. Structural requirements of the flavin side chain. Biochem 1973 12 1482-91. 

Mager HIX, Sazou D, Liu YH, Tu S-C, Kadish KM. Reversible one-electron generation of 4 5-substituted flavin radical cations Models for a postulated key intermediate in bacterial bioluminescence. J Am Chem Soc 1988 110 3759-62. 

Balny, C., and Hastings, J. W. (1975). Fluorescence and bioluminescence of bacterial luciferase intermediates. Biochemistry 14 4719-4723. 

Although in some cases an energy-transfer step may be involved, the specific emitter in a bioluminescent reaction is generally an intermediate or product whose excited state is populated during the reaction. Free flavin in aqueous solution has a fluorescence emission maximum at 525 nm, while bacterial luminescence both in vivo and in vitro emits at a maximum around 495 nm. These results and their implications are reported and discussed elsewhere (Balny and Hastings, 1975). 

Lee J, O Kane D, Gibson B. Bioluminescence spectral and fluorescence dynamics study of the interaction of lumazine protein with the intermediates of bacterial luciferase bioluminescence. Biochemistry 1989 28 4263-71. 

Bacteria A peroxide intermediate, quorum sensing and milky seas. Although the luciferin-luciferase test in bacterial extracts was negative, Strehler16 discovered that light emission in extracts could be obtained by adding reduced pyridine nucleotide, underlining the fact that bioluminescence is not a phenomenon separate... 

Cho, K.-W. and Lee, H.-J., Nature of high energy intermediate involved in the bioluminescence reaction catalyzed by bacterial luciferase, Korean Biochem. J., 17, 1,1984. 

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