Bacterial luminescence

In addition to hexadecanal, Cormier and Strehler (1953) discovered that homologous aldehydes, such as decanal and dodecanal, were also active in stimulating bacterial luminescence. Thus, they showed that bacterial luminescence requires a saturated long-chain aldehyde, but the specific aldehyde that is actually involved in the in vivo luminescence remained unknown for the next 20 years. 

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. 

Another notable feature of the in vivo bacterial luminescence is seen in their emission spectra. Although the emission peak of in vitro bacterial luminescence is normally at about 490 nm, the in vivo emission peaks of various bacterial species and strains are significantly shifted from 490 nm, ranging from the shortest wavelength of 472 nm to over 500 nm. Some expanded notes concerning in vivo bacterial luminescence are given below. 

Fig. 2.4 The spectrum of bacterial luminescence measured with B. harveyi luciferase, FMN, tetradecanal and NADH, in 50 mM phosphate buffer, pH 7.0, at 0°C (dashed line from Matheson et al., 1981) and the absorption and fluorescence emission spectra of LumP (solid lines) and Rf-LumP (dotted lines) obtained from P. leiog-natbi, in 25 mM phosphate buffer, pH 7.0, containing 1 mM EDTA and 10 mM 2-mercaptoethanol, at room temperature (from Petushkov et al, 2000, with permission from Elsevier). LumP is a lumazine protein, and Rf-LumP contains riboflavin instead of lumazine in the lumazine protein. Fluorescence emission curves are at the right side of the absorption curves.

Cormier, M. J., and Totter, J. R. (1957). Quantum efficiency determinations on components of the bacterial luminescence system. Biochim. Biophys. Acta 25 229-237. 

Dunlap, P. V. (1991). Organization and regulation of bacterial luminescence genes. Photochem. Photobiol. 54 1157-1170. 

Ulitzur, S. (1989). The regulatory control of the bacterial luminescence system — a new view.. Biolumin. Chemilumin. 4 317-325. 

Ulitzur, S., and Hastings, J. W. (1979a). Evidence for tetradecanal as the natural aldehyde in bacterial luminescence. Proc. Natl. Acad. Sci. USA 76 265-267. 

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

FMNH2 requirement in bacterial luminescence Crystallization of Cypridina luciferin Crystallization of firefly luciferin Cypridina luciferin in fishes the first cross reaction discovered Structure of firefly luciferin Discovery of aequorin and GFP (green fluorescent protein) Structure of Cypridina luciferin Concept of photoprotein Structure of Latia luciferin Dioxetanone mechanism proposed in firefly and Cypridina luminescence... 

The first steps in bypassing of the biological, technological, and financial burden of live stock culturing or maintenance were made more than 20 years ago through the development of a bacterial luminescence inhibition test [34,35] this bioassay is presently known and used worldwide as the Microtox test. The revolutionary principle of this test is that it uses a lyophihzed strain of a (marine) bacterium Photobacterium phosphoreum). This makes the bioassay apphcable anytime, anywhere, without the need for continuous culturing of the test species. 

Hyan C-K,TamiyaE,TakeuchiT, Karube I (1993) A novel BOD sensor based on bacterial luminescence. Biotechnol Bioeng 41 1107-1111... 

Riisberg, M., Bratlie, E. and Stenersen, J. (1996) Comparison of the response of bacterial luminescence and mitochondrial respiration to the effluent of an oil refinery, Environmental Toxicology and Chemistry 15 (4), 501-502. 

Ross, P. (1993) The use of bacterial luminescence systems in aquatic toxicity testing, in M. Richardson (ed.), Ecotoxicology Monitoring, VCH Publishers, Weinheim, Germany, pp. 185-195. 

Vibrio fischeri, bacterial luminescence inhibition test or Microtox assay (DEVL34, 1998). 

Bulich, A.A., M.W. Greene, and D.L. Isenberg. 1981. Reliability of the bacterial luminescence bioassay for the determination of toxicity of pure compounds and complex effluents. In D.R. Branson and K.L. Dickson (eds), Aquatic Toxicology and Hazard Assessment Fourth Conference, pp. 338-347. Baltimore, USA ASTM STP737. 

Wolska, L. andZ. Polkowska. 2001. Bacterial luminescence test screening of highly polluted areas in the Odra River. Bull. Environ. Contam. Toxicol. 67 52-58. 

Chaiyen P. LuxG is a functioning flavin reductase for bacterial luminescence. J. Bacteriol. 2008 190 1531-1538. 20. 

Nealson KH, Platt T, Hastings JW. Cellular control of the synthesis and activity of the bacterial luminescent system. J. Bacteriol. 1970 104 313-322. 

The bacterial luminescence toxicity assay Micro-tox Vibrio fischeri) has achieved international recognition for its usefulness in detecting acute and chronic aqueous toxicity that correlates with... 

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). 

Bacterial luminescence inhibition assay on Vibrio fischeri (formerly Photobacterium phosphoreum). 

McElroy WD, Deluca MA. Firefly and bacterial luminescence Basic science and applications. J Applied Biochem 1983 5 197-209. 

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