Isolation and characterization of the transient, luciferase-bound flavin-4a-hydroxide in the bacterial luciferase reaction

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ghislascan154.pdf
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1987
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Kurfürst, Manfred
Macheroux, Peter
Hastings, J. Woodland
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Biochimica et Biophysica Acta. 1987, 924(1), pp. 104-110. ISSN 0304-4165. Available under: doi: 10.1016/0304-4165(87)90076-6
Zusammenfassung

Procedures and conditions have been established such that the unstable enzyme-bound flavin intermediate produced in the bacterial luciferase reaction can be isolated as approximately 70% of the flavin product, the remaining being the final product, FMN. The structure of the intermediate is proposed to be that of a luciferase-bound 4a,5-dihydroflavin-4a-hydroxide. The intermediate has a half-life of 33 min at 2°C and decays spontaneously to give H2O and luciferase-bound FMN with an activation enthalpy of about 120 kJ/mol. It has an absorption spectrum (λmax = 360 nm) that is consistent with the proposed structure, and a fluorescence emission (λmax = 485 nm) that matches the bioluminescence emission closely.

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Fachgebiet (DDC)
570 Biowissenschaften, Biologie
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Bioluminescence, Oxygen activation, Flavin intermediate, Luciferase, Bacteria
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ISO 690KURFÜRST, Manfred, Peter MACHEROUX, Sandro GHISLA, J. Woodland HASTINGS, 1987. Isolation and characterization of the transient, luciferase-bound flavin-4a-hydroxide in the bacterial luciferase reaction. In: Biochimica et Biophysica Acta. 1987, 924(1), pp. 104-110. ISSN 0304-4165. Available under: doi: 10.1016/0304-4165(87)90076-6
BibTex
@article{Kurfurst1987Isola-7258,
  year={1987},
  doi={10.1016/0304-4165(87)90076-6},
  title={Isolation and characterization of the transient, luciferase-bound flavin-4a-hydroxide in the bacterial luciferase reaction},
  number={1},
  volume={924},
  issn={0304-4165},
  journal={Biochimica et Biophysica Acta},
  pages={104--110},
  author={Kurfürst, Manfred and Macheroux, Peter and Ghisla, Sandro and Hastings, J. Woodland}
}
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    <dcterms:abstract xml:lang="eng">Procedures and conditions have been established such that the unstable enzyme-bound flavin intermediate produced in the bacterial luciferase reaction can be isolated as approximately 70% of the flavin product, the remaining being the final product, FMN. The structure of the intermediate is proposed to be that of a luciferase-bound 4a,5-dihydroflavin-4a-hydroxide. The intermediate has a half-life of 33 min at 2°C and decays spontaneously to give H2O and luciferase-bound FMN with an activation enthalpy of about 120 kJ/mol. It has an absorption spectrum (λmax = 360 nm) that is consistent with the proposed structure, and a fluorescence emission (λmax = 485 nm) that matches the bioluminescence emission closely.</dcterms:abstract>
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