The role of protein globule in firefly luciferase catalysis

The important role of the dynamic structure of firefly luciferase in enzyme functioning is a subject of this literature review. Due to the domain alternation, the optimal configuration of the active site is created for each stage of the luciferin oxidation. The diversity of bioluminescence spectra i...

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Published inPhotochemistry and photobiology Vol. 100; no. 5; pp. 1191 - 1199
Main Authors Ugarova, Natalia N., Lomakina, Galina Yu
Format Journal Article
LanguageEnglish
Published United States Blackwell Publishing Ltd 01.09.2024
Subjects
Bioluminescence
Catalysis
Emission spectra
Emitters
Excitation spectra
Literature reviews
Luciferin
Oxidation
Protein structure
Proteins
Spectral emittance
Thermal stability
luciferin
bioluminescence spectra
bioluminescence
oxyluciferin
thermostability
domain alternation mechanism
luciferase conformers
firefly luciferase
Online AccessGet full text
ISSN0031-8655
1751-1097
1751-1097
DOI10.1111/php.13909

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Abstract The important role of the dynamic structure of firefly luciferase in enzyme functioning is a subject of this literature review. Due to the domain alternation, the optimal configuration of the active site is created for each stage of the luciferin oxidation. The diversity of bioluminescence spectra is explained by the combined emission of several coexisting forms of electronically excited oxyluciferin. The superposition of two or three emitter forms recorded in the bioluminescence spectra indicates that different luciferase conformers coexist in the reaction medium in dynamic equilibrium. The relationship between the thermal stability of the protein globule and the bioluminescence spectra is also discussed
AbstractList The important role of the dynamic structure of firefly luciferase in enzyme functioning is a subject of this literature review. Due to the domain alternation, the optimal configuration of the active site is created for each stage of the luciferin oxidation. The diversity of bioluminescence spectra is explained by the combined emission of several coexisting forms of electronically excited oxyluciferin. The superposition of two or three emitter forms recorded in the bioluminescence spectra indicates that different luciferase conformers coexist in the reaction medium in dynamic equilibrium. The relationship between the thermal stability of the protein globule and the bioluminescence spectra is also discussed.The important role of the dynamic structure of firefly luciferase in enzyme functioning is a subject of this literature review. Due to the domain alternation, the optimal configuration of the active site is created for each stage of the luciferin oxidation. The diversity of bioluminescence spectra is explained by the combined emission of several coexisting forms of electronically excited oxyluciferin. The superposition of two or three emitter forms recorded in the bioluminescence spectra indicates that different luciferase conformers coexist in the reaction medium in dynamic equilibrium. The relationship between the thermal stability of the protein globule and the bioluminescence spectra is also discussed.
The important role of the dynamic structure of firefly luciferase in enzyme functioning is a subject of this literature review. Due to the domain alternation, the optimal configuration of the active site is created for each stage of the luciferin oxidation. The diversity of bioluminescence spectra is explained by the combined emission of several coexisting forms of electronically excited oxyluciferin. The superposition of two or three emitter forms recorded in the bioluminescence spectra indicates that different luciferase conformers coexist in the reaction medium in dynamic equilibrium. The relationship between the thermal stability of the protein globule and the bioluminescence spectra is also discussed.
The important role of the dynamic structure of firefly luciferase in enzyme functioning is a subject of this literature review. Due to the domain alternation, the optimal configuration of the active site is created for each stage of the luciferin oxidation. The diversity of bioluminescence spectra is explained by the combined emission of several coexisting forms of electronically excited oxyluciferin. The superposition of two or three emitter forms recorded in the bioluminescence spectra indicates that different luciferase conformers coexist in the reaction medium in dynamic equilibrium. The relationship between the thermal stability of the protein globule and the bioluminescence spectra is also discussed
Author Ugarova, Natalia N.
Lomakina, Galina Yu
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  givenname: Galina Yu
  surname: Lomakina
  fullname: Lomakina, Galina Yu
  organization: Faculty of Chemistry Lomonossov Moscow State University Moscow Russia, Bauman Moscow State Technical University Moscow Russia
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Issue 5
Keywords luciferin
bioluminescence spectra
bioluminescence
oxyluciferin
thermostability
domain alternation mechanism
luciferase conformers
firefly luciferase
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Snippet The important role of the dynamic structure of firefly luciferase in enzyme functioning is a subject of this literature review. Due to the domain alternation,...
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SubjectTerms Bioluminescence
Catalysis
Emission spectra
Emitters
Excitation spectra
Literature reviews
Luciferin
Oxidation
Protein structure
Proteins
Spectral emittance
Thermal stability
Title The role of protein globule in firefly luciferase catalysis
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