Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1980 Jan;77(1):249–252. doi: 10.1073/pnas.77.1.249

Physical interaction and activity coupling between two enzymes induced by immobilization of one.

S C Tu, J W Hastings
PMCID: PMC348246  PMID: 6965792

Abstract

Flavin reductase and bacterial luciferase are believed to be coupled in the in vivo light emitting reaction. In extracts, however, they are both soluble enzymes that exhibit little or no association. Immobilized luciferase, covalently attached to Sepharose, was found to bind the soluble reductase and to exhibit activity in the coupled reaction reaction with an enhanced efficiency of electron transfer.

Full text

PDF
249

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Baldwin T. O., Hastings J. W., Riley P. L. Proteolytic inactivation of the luciferase from the luminous marine bacterium Beneckea harveyi. J Biol Chem. 1978 Aug 25;253(16):5551–5554. [PubMed] [Google Scholar]
  2. Cline T. W., Hastings J. W. Mutationally altered bacterial luciferase. Implications for subunit functions. Biochemistry. 1972 Aug 29;11(18):3359–3370. doi: 10.1021/bi00768a008. [DOI] [PubMed] [Google Scholar]
  3. Duane W., Hastings J. W. Flavin mononucleotide reductase of luminous bacteria. Mol Cell Biochem. 1975 Jan 31;6(1):53–64. doi: 10.1007/BF01731866. [DOI] [PubMed] [Google Scholar]
  4. Friedland J., Hastings J. W. Nonidentical subunits of bacterial luciferase: their isolation and recombination to form active enzyme. Proc Natl Acad Sci U S A. 1967 Dec;58(6):2336–2342. doi: 10.1073/pnas.58.6.2336. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. GIBSON Q. H., HASTINGS J. W. The oxidation of reduced flavin mononucleotide by molecular oxygen. Biochem J. 1962 May;83:368–377. doi: 10.1042/bj0830368. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gunsalus-Miguel A., Meighen E. A., Nicoli M. Z., Nealson K. H., Hastings J. W. Purification and properties of bacterial luciferases. J Biol Chem. 1972 Jan 25;247(2):398–404. [PubMed] [Google Scholar]
  7. HASTINGS J. W., GIBSON Q. H. Intermediates in the bioluminescent oxidation of reduced flavin mononucleotide. J Biol Chem. 1963 Jul;238:2537–2554. [PubMed] [Google Scholar]
  8. HASTINGS J. W., RILEY W. H., MASSA J. THE PURIFICATION PROPERTIES, AND CHEMILUMINESCENT QUANTUM YIELD OF BACTERIAL LUCIFERASE. J Biol Chem. 1965 Mar;240:1473–1481. [PubMed] [Google Scholar]
  9. HASTINGS J. W., SPUDICH J., MALNIC G. THE INFLUENCE OF ALDEHYDE CHAIN LENGTH UPON THE RELATIVE QUANTUM YIELD OF THE BIOLUMINESCENT REACTION OF ACHROMOBACTER FISCHERI. J Biol Chem. 1963 Sep;238:3100–3105. [PubMed] [Google Scholar]
  10. Hastings J. W., Nealson K. H. Bacterial bioluminescence. Annu Rev Microbiol. 1977;31:549–595. doi: 10.1146/annurev.mi.31.100177.003001. [DOI] [PubMed] [Google Scholar]
  11. Hastings J. W., Weber K., Friedland J., Eberhard A., Mitchell G. W., Gunsalus A. Structurally distinct bacterial luciferases. Biochemistry. 1969 Dec;8(12):4681–4689. doi: 10.1021/bi00840a004. [DOI] [PubMed] [Google Scholar]
  12. Jablonski E., DeLuca M. Purification and properties of the NADH and NADPH specific FMN oxidoreductases from Beneckea harveyi. Biochemistry. 1977 Jun 28;16(13):2932–2936. doi: 10.1021/bi00632a020. [DOI] [PubMed] [Google Scholar]
  13. Jablonski E., DeLuca M. Studies of the control of luminescence in Beneckea harveyi: properties of the NADH and NADPH:FMN oxidoreductases. Biochemistry. 1978 Feb 21;17(4):672–678. doi: 10.1021/bi00597a018. [DOI] [PubMed] [Google Scholar]
  14. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  15. Meighen E. A., Nicoli M. Z., Hastings J. W. Functional differences of the nonidentical subunits of bacterial luciferase. Properties of hybrids of native and chemically modified bacterial luciferase. Biochemistry. 1971 Oct 26;10(22):4069–4073. doi: 10.1021/bi00798a009. [DOI] [PubMed] [Google Scholar]
  16. Michaliszyn G. A., Wing S. S., Meighen E. A. Purification and properties of a NAD(P)H:flavin oxidoreductase from the luminous bacterium, Beneckea harveyi. J Biol Chem. 1977 Nov 10;252(21):7495–7499. [PubMed] [Google Scholar]
  17. Mitchell G. W., Hastings J. W. A stable, inexpensive, solid-state photomultiplier photometer. Anal Biochem. 1971 Jan;39(1):243–250. doi: 10.1016/0003-2697(71)90481-7. [DOI] [PubMed] [Google Scholar]
  18. Mosbach K., Mattiasson B. Multistep enzyme systems. Methods Enzymol. 1976;44:453–478. doi: 10.1016/s0076-6879(76)44033-8. [DOI] [PubMed] [Google Scholar]
  19. Ne'eman Z., Ulitzur S., Branton D., Hastings J. W. Membrane polypeptides co-induced with the bacterial bioluminescent system. J Biol Chem. 1977 Jul 25;252(14):5150–5154. [PubMed] [Google Scholar]
  20. Nicoli M. Z., Meighen E. A., Hastings J. W. Bacterial luciferase. Chemistry of the reactive sulfhydryl. J Biol Chem. 1974 Apr 25;249(8):2385–2392. [PubMed] [Google Scholar]
  21. Porath J., Axén R. Immobilization of enzymes to agar, agarose, and Sephadex supports. Methods Enzymol. 1976;44:19–45. doi: 10.1016/s0076-6879(76)44005-3. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES