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The effect of camphor on bacterial bioluminescence

  • Vadim Danilov
  • Nina Baranova
  • Anvar Ismailov
  • Nicolai Egorov
Applied Microbiology

Summary

The inhibitory effect of camphor on bioluminescence of both bacteria and bacterial luciferase has been examined. The camphor has been shown to be a substrate of cytochrome P-450 of the luminous bacteria Photobacterium fischeri. The inhibition of the luminescence reaction provided evidence for the competitive nature of the interaction of camphor and aliphatic aldehyde at the binding site for luciferase. Camphor is also supposed to interact with P-450. The findings indicate that the hydroxylation process of camphor affects the kinetics of the luminescence.

Keywords

Aldehyde Camphor Aliphatic Aldehyde Competitive Nature Luminous Bacterium 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Baranova NA, Ismailov AD, Egorov NS, Danilov VS (1980a) Cytochromes of the luminous bacteria Photobacterium fischeri. Solubilization and dependency on the luminescence. Mikrobiologia USSR 49:477–482Google Scholar
  2. Baranova NA, Alexandrushkina NA, Egorov NS (1980b) Cultural and physiologo-biochemical properties of the luminous bacteria Photobacterium fischeri. Biol Nauki USSR 12:47–49Google Scholar
  3. Danilov VS (1979) On the mechanism of the bioluminescence of bacteria. Dokl Acad Nauk USSR 249:477–479Google Scholar
  4. Gunsalus C, Meeks JR, Lipscomb JD, Debrunner P, Münck E (1974) Bacterial monooxygenases — the P-450 cytochrome sysrem. In: Hayaishi O (ed) Molecular Mechanism of Oxygen Activation. Academic Press, New York, pp 559–613Google Scholar
  5. Gunsalus C, Pederson TC, Sligar SG (1975) Oxygenase-catalysed biological hydroxylations. Ann Rev Biochem 44:377–388Google Scholar
  6. Gunsalus C, Sligar SG (1978) Oxygen reduction by the P-450 monooxygenase systems. Adv Enzymol 47:1–44Google Scholar
  7. Hastings JW (1968) Bioluminescence. Ann Rev Biochem 37:597–630Google Scholar
  8. Hastings JW, Nealson KH (1978) Light emission in the mixed function oxidation of reduced flavin and fatty aldehyde. CRC Critical Rev in Biochemistry 5:163–184Google Scholar
  9. Ismailov AD, Baranova NA, Egorov NS, Danilov VS (1980) Electrontransport chains Photobacterium fischeri. Mikrobiologia USSR 49:377–382Google Scholar
  10. Leibman KC, Hildebrandt AG, Estabrook RW (1969) Spectrophotometric studies of interaction between various substrates in their binding to microsomal cytochrome P-450. Biochem Biophys Res Commun 36:789–794Google Scholar
  11. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the folin phenol reagent. J Biol Chem 193: 265–275Google Scholar
  12. Omura T, Sato R (1964) The carbon monoxide-binding pigment of liver microsomes. I Evidence for its hemoprotein nature. J Biol Chem 239:2370–2378Google Scholar
  13. Orrenius S, Kupfer D, Ernster L (1970) Substrate binding to cytochrome P-450 of liver and adrenal microsomes. FEBS Letters 6:249–252Google Scholar
  14. Reichelt JL, Baumann P (1973) Taxonomy of the marine luminous bacteria. Arch Microbiol 94:283–330Google Scholar
  15. Schumichin VN, Danilov VS, Malkov YA, Egorov NS (1980a) Preparation and purification of bacterial luciferase Photobacterium fischeri. Biochimia USSR 45:1325–1330Google Scholar
  16. Schumichin VN, Danilov VS, Egorov NS (1980b) Some peculiarities of the structure-functional mode of luciferase Photobacterium fischeri. Bioorganicheskaya khimia USSR 6, 5: 765–772Google Scholar

Copyright information

© Springer-Verlag 1982

Authors and Affiliations

  • Vadim Danilov
    • 1
  • Nina Baranova
    • 1
  • Anvar Ismailov
    • 1
  • Nicolai Egorov
    • 1
  1. 1.Microbiological DepartmentM. V. Lomonosov State UniversityMoscowUSSR

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