Bioluminescence: pH Activity Profies of Related Luciferase Fractions

@article{Krieger1968BioluminescencePA,
  title={Bioluminescence: pH Activity Profies of Related Luciferase Fractions},
  author={Neil Reese Krieger and John Woodland Hastings},
  journal={Science},
  year={1968},
  volume={161},
  pages={586 - 589}
}
The 27, 000g supernatant from crude extracts of the dinoflagellate Gonyaulax can be fractionated into two components having luciferase activity that differ both in molecular weight (35, 000 and 150, 000) and in pH activity profile. The smaller component has activity over a broad range from pH 5 to 9, while the larger one is active only in the acid region. This clarifies the previous ambiguity in the literature regarding the optimum pH for the assay of luciferase. 

A substrate-binding protein in the Gonyaulax bioluminescence reaction.

C-terminal region of the active domain enhances enzymatic activity in dinoflagellate luciferase.

  • Chie Suzuki-OgohChun WuY. Ohmiya
  • Biology, Chemistry
    Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology
  • 2008
TLDR
The results indicate that the C-terminal region of this enzyme could be important for the bioluminescence reaction, although based on crystal structure of the luciferase domain, this region does not contain active or regulatory sites.

Dinoflagellate bioluminescence: A comparative study of invitro components

TLDR
In vitro bioluminescence components of the dinoflagellates Gonyaulax polyedra, G. tamarensis, Dissodinium lunula, and Pyrocystis noctiluca were studied and the observations that D. lunula and P. noCTiluca apparently lack LBP and have luciferases with low MW single chains require further clarification.

A circadian rhythm of the luciferin binding protein fromGonyaulax polyedra

TLDR
A procedure for the determination of the dissociation constant (Kd) of the luciferin binding protein (LBP) is presented, and Kd is estimated to be 7×10−9 M at pH 8.0, assuming an overall quantum yield of 0.1 for the bioluminescent reaction.

Solubilization of molecular elements of scintillons: Bioluminescent particles from dinoflagellates

TLDR
The results suggest that the substrate-binding protein is bound to the particle chiefly by electrostatic forces, whereas the attachment of luciferase involves instead hydrophobic interactions, and that the two are present in the particles in approximately equal amounts.

Cloning and Characterization of an Active Fragment of Luciferase from a Luminescent Marine Alga, Pyrocystis lunula¶

TLDR
The pH–activity profile and the bioluminescence spectrum of the recombinant enzyme having a third domain are almost identical to those of an extract from P. lunula cultured in vitro, suggesting that histidine residues could be responsible for pH-sensitivity in dinoflagellate luciferase.

Cloning and Characterization of an Active Fragment of Luciferase from a Luminescent Marine Alga, Pyrocystis lunula ¶

TLDR
The pH–activity profile and the bioluminescence spectrum of the recombinant enzyme having a third domain are almost identical to those of an extract from P. lunula cultured in vitro, suggesting that histidine residues could be responsible for pH‐sensitivity in dinoflagellate luciferase.

Characterization and crystallization of active domains of a novel luciferase from a marine dinoflagellate.

TLDR
Two domains of Lingulodinium polyedrum luciferase, a bioluminescent protein found in the marine dinoflagellate formerly known as Gonyaulax, have been cloned, expressed and crystallized.

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The luminescent reaction in extracts of the marine dinoflagellate, Gonyaulax polyedra.

Supported by a grant from the National Science Foundation (GB-5427) and a contract from the Office of Naval Research (N00014). We thank Dr

    K. is a predoctoral fellow, National Institutes of Health