Bacterial luciferase reaction

Abu-Soud, H., Mullins, L. S., Baldwin, T. O., and Raushel, F. M. (1992). Stopped-flow kinetic analysis of the bacterial luciferase reaction. Biochemistry 31 3807-3813. 

Kurfuerst, M., Macheroux, P., Ghisla, S., and Hastings, J. W. (1987). Isolation and characterization of the transient, luciferase-bound flavin-4a-hydroxide in the bacterial luciferase reaction. Biochim. Biophys. Acta 924 104-110. 

Sirokman, G., Wilson, T., and Hastings, J. W. (1995). A bacterial luciferase reaction with a negative temperature coefficient attributable to protein-protein interaction. Biochemistry 34 13074-13081. 

Macheroux P, Ghisla S, Hastings JW. Spectral detection of an intermediate preceding the excited-state in the bacterial luciferase reaction. Biochemistry 1993 32 4183 186. 

Fig. 14.35 Examples of various luminescent (C) The luminol reaction with horseradish reactions. (A) The firefly Luciferase reaction. peroxidase catalyst. (D) The electrolumines-(B) The bacterial luciferase reaction. cence of Ru(bpy)3.

Macheroux, R, Ghisla, S., Kurfiirst, M., and Hastings, J.W., Studies on the bacterial luciferase reaction isotope effects on the Hght emission. Is a CIEEL mechanism involved , in Flavins and Flavoproteins, Bray, R.C., Engel, PC., and Mayhew, S.G., Eds., Walter deGruyter, Berlin, 1984, p. 669. 

Wada, N., Hastings, J.W, and Watanabe, H., Superoxide anion reacts with enzyme intermediate in the bacterial luciferase reaction competitive with intramolecular electron transfer, /. Biolumin. Chemilumin., 12,15,1997. 

Francisco, W.A., Abu-Soud, H.M., DelMonte, A.J., Singleton, D.A., Baldwin, TO., and Raushel, F.M., Deuterium kinetic isotope effects and the mechanism of the bacterial luciferase reaction. 

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.

The reported quantum yields of the long-chain aldehydes in the luminescence reaction catalyzed by P. fischeri luciferase are 0.1 for dodecanal with the standard I (Lee, 1972) 0.13 for decanal with the standard I (McCapra and Hysert, 1973) and 0.15-0.16 for decanal, dodecanal and tetradecanal with the standard III (Shimomura et al., 1972). Thus, the quantum yield of long-chain aldehydes in the bacterial bioluminescence reaction appears to be in the range of 0.10-0.16. 

Eckstein, J. W., and Ghisla, S. (1991). On the mechanism of bacterial luciferase. 4a,5-Dihydroflavins as model compounds for reaction intermediates. In Flavins Flavoproteins, Proc. Int. Symp., 10th, 1990, 269-272. 

Eley, M., et al. (1970). Bacterial bioluminescence. Comparisons of bioluminescence emission spectra, the fluorescence of luciferase reaction mixtures, and the fluorescence of flavin cations. Biochemistry 9 2902-2908. 

Lei, B., Ding, Q., and Tu, S.-C. (2004). Identity of the emitter in the bacterial luciferase luminescence reaction binding and fluorescence quantum yield studies of 5-decyl-4a-hydroxy-4a,5-dihydroriboflavin-5 -phosphate as a model. Biochemistry 43 15975-15982. 

Sakharov, G. N., Ismailov, A. D., and Danilov, V. S. (1988). Temperature dependencies of the reaction of bacterial luciferases from Beneckea har-veyi and Photobacterium fischeri. Biokhimiya 53 891-898. 

Sinclair, J. F., Waddle, J. J., Waddill, E. F., and Baldwin, T. O. (1993). Purified native subunits of bacterial luciferase are active in the bioluminescence reaction but fail to assemble into the a(3 structure. Biochemistry 32 5036-5044. 

Strehler, B. L., and Cormier, M. J. (1954). Isolation, identification, and function of long chain fatty aldehydes affecting the bacterial luciferin-luciferase reaction. J. Biol. Chem. 211 213-225. 

Watanabe, H., Nagoshi, T., and Inaba, H. (1993). Luminescence of a bacterial luciferase intermediate by reaction with H2O2 the evolutionary origin of luciferase and source of endogenous light emission. Biochim. Biophys. Acta 1141 297-302. 

Bacterial bioluminescence, 30-46 factors required, 31 general scheme, 32 in vivo luminescence, 41 luminescence reaction, 37, 38 Bacterial luciferase, 33-35, 343 assay, 39 cloning, 34 crystal structure, 34 extraction and purification, 34 inactivation, 34, 35 molecular weight, 34 properties, 34 storage, 35 subunits, 34... 

Discovery of luciferin-luciferase reaction Benzoylation of Cypridina luciferin ATP requirement in firefly luminescence Requirement for long-chain aldehyde (luciferin) in bacterial luminescence... 

The bacterial bioluminescent reaction is also catalyzed by a luciferase (EC 1.14.14.3) isolated from marine bacteria. The four most studied types are Vibrio harveyi, Vibrio fischeri, Photobacterium phosphoreum and Photobacterium leiognathi18, 19. In these different luminescent bacteria the... 

The possibility of isolating the components of the two above-reported coupled reactions offered a new analytical way to determine NADH, FMN, aldehydes, or oxygen. Methods based on NAD(P)H determination have been available for some time and NAD(H)-, NADP(H)-, NAD(P)-dependent enzymes and their substrates were measured by using bioluminescent assays. The high redox potential of the couple NAD+/NADH tended to limit the applications of dehydrogenases in coupled assay, as equilibrium does not favor NADH formation. Moreover, the various reagents are not all perfectly stable in all conditions. Examples of the enzymes and substrates determined by using the bacterial luciferase and the NAD(P)H FMN oxidoreductase, also coupled to other enzymes, are listed in Table 5. 

Bioluminescent reactions are also employed for imaging purposes, in particular the firefly and the bacterial luciferin/luciferase ones (Fig. 1). The firefly luciferin/luciferase reaction requires ATP, magnesium ions, and oxygen. Many different luciferins and mutant luciferases have been investigated to optimize the... 

Figure 2 Effect of enzyme immobilization on luminescent image spatial resolution evaluated using coupled enzymatic reactions on nylon net as a model system, (a) Immobilized 3a-hydroxysteroid dehydrogenase (b) immobilized 3a-hydroxysteroid dehydrogenase and FMN-NADH oxidoreductase (c) immobilized 3a-hydroxysteroid dehydrogenase, FMN-NADH oxidoreductase, and bacterial luciferase. (From Ref. 47. Copyright John Wiley Sons Ltd. Reproduced with permission.)...

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