Luciferases bacterial

Bioluminescence can also be used as the basis for immunoassay. For example, bacterial luciferase has been used in a co-immobilized system to detect and quantify progesterone using a competitive immunoassay format (34), and other luciferase-based immunoassays have been used to quantify insulin, digoxin, biotin, and other clinically important analytes (35). 

The biochemical mechanism of bacterial luminescence has been studied in detail and reviewed by several authors (Hastings and Nealson, 1977 Ziegler and Baldwin, 1981 Lee et al., 1991 Baldwin and Ziegler, 1992 Tu and Mager, 1995). Bacterial luciferase catalyzes the oxidation of a long-chain aldehyde and FMNH2 with molecular oxygen, thus the enzyme can be viewed as a mixed function oxidase. The main steps of the luciferase-catalyzed luminescence are shown in Fig. 2.1. Many details of this scheme have been experimentally confirmed. 

AbouKhair, N. K., Ziegler, M. M., and Baldwin, T. O. (1984). The catalytic turnover of bacterial luciferase produces a quasi-stable species of altered conformation. In Bray, R. C., et al. (eds.), Flavins Flavoproteins, Proc. Int. Symp., 8th, pp. 371-374. de Gruyter, Berlin. 

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. 

Baldwin, T. O., et al. (1987). Applications of the cloned bacterial luciferase genes luxA and luxB to the study of transcriptional promoters and terminators. In Schoelmerich, J. (ed.), Biolumin. Chemilumin., Proc. Int. Biolumin. Chemilumin. Symp., 4th, 1986, pp. 373-376. Wiley, Chichester, UK. 

Baldwin, T. O., etal. (1989). Site-directed mutagenesis of bacterial luciferase analysis of the essential thiol. J. Biolumin. Chemilumin. 4 40-48. 

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

Cohn, D. H., et al. (1985). Nucleotide sequence of the luxA gene of Vibrio harveyi and the complete amino acid sequence of the a subunit of bacterial luciferase. J. Biol. Chem. 260 6139-6146. 

Cousineau, J., and Meighen, E. A. (1976). Chemical modification of bacterial luciferase with ethoxyformic anhydride evidence for an essential histidyl residue. Biochemistry 15 4992-5000. 

Danilov, V. S., and Maikov, Y. A. (1984). Bacterial luciferase from Beneckea harveyi — an iron-containing enzyme. Dokl. Akad. Nauk SSSR 275 206-209. 

Eberhard, A. (1972). Inhibition and activation of bacterial luciferase synthesis. J. Bacteriol. 109 1101-1105. 

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. 

Escher, A., O Kane, D. J., Lee, J., and Szalay, A. A. (1989). Bacterial luciferase a(3 fusion protein is fully active as a monomer and highly sensitive in vivo to elevated temperature. Proc. Natl. Acad. Sci. USA 86 6528-6532. 

Flynn, G. C., Beckers, C. J. M., Baase, W. A., and Dahlquist, F. W. (1993). Individual subunits of bacterial luciferase are molten globules and interact with molecular chaperones. Proc. Natl. Acad. Sci. USA 90 10826-10830. 

Francisco, W. A., et al. (1996). Interaction of bacterial luciferase with 8-substituted flavin mononucleotide derivatives. /. Biol. Chem. 271 104-110. 

Hastings, J. W., et al. (1969a). Structurally distinct bacterial luciferase. Biochemistry 8 4681-4689. 

Holzman, T. F., and Baldwin, T. O. (1982). Isolation of bacterial luciferases by affinity chromatography on 2,2-diphenylpropylamine-Sepharose phosphate-mediated binding to immobilized substrate analogue. Biochemistry 21 6194-6201. 

Jockers, R., Ziegler, T., and Schmid, R. D. (1995). Interaction between aldehyde derivatives and the aldehyde binding site of bacterial luciferase. ]. Biolumin. Chemilumin. 10 21-27. 

Kaaret, T. W., and Bruice, T. C. (1990). Electrochemical luminescence with N(5)-ethyl-4a-hydroxy-3-methyl-4a,5-dihydrolumiflavin. The mechanism of bacterial luciferase. Photochem. Photobiol. 51 629-633. 

Kurfuerst, M., Macheroux, P., Ghisla, S., and Hastings, J. W. (1989). Bioluminescence emission of bacterial luciferase with 1 -deaza-FMN. Evidence for the noninvolvement of N(l)-protonated flavin species as emitters. Eur. J. Biochem. 181 453 157. 

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