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Cited by 18bioluminescence and chemiluminescence researchEnzyme Catalysis and ImmobilizationProtein Structure and Dynamics

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Relationship between stability and bioluminescence color of firefly luciferase

Maghami, Parvaneh, Ranjbar, Bijan, Hosseinkhani, Saman, Ghasemi, Atiyeh, Moradi, Ali, Gill, Pooria·2010·Photochemical & Photobiological Sciences
DOI 10.1039/b9pp00161a
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Abstract

Firefly luciferase catalyzes the oxidation of luciferin in the presence of ATP, Mg(2+) and molecular oxygen. The bioluminescence color of firefly luciferases is identified by the luciferase structure and assay conditions. Amongst different types of beetles, luciferase from Phrixotrix railroad worm (PhRE) with a unique additional residue (Arg353) naturally emits red bioluminescence color. By insertion of Arg356 in luciferase of Lampyris turkestanicus, corresponding to Arg353 in Phrixotrix hirtus, the color of the emitted light was changed to red. To understand the effect of this position on the bioluminescence color shift, four residues with similar sizes but different charges (Arg, Lys, Glu, and Gln) were inserted into Photinus pyralis luciferase. Comparison of mutants with native luciferase shows that mutation brought an increase in the content of secondary structure and globular compactness of (P. pylalis) luciferase. Comparative study of chemical denaturation of native and mutant luciferases by activity measurement, intrinsic and extrinsic fluorescence, circular dichroism, and DSC techniques revealed that insertion of positively charged residues (Arg, Lys) in the flexible loop (352-358) plays a significant role on the stability of (P. pyralis) luciferase and changes the light color to red.

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Metadata

Authors
Maghami, P., Ranjbar, B., Hosseinkhani, S., Ghasemi, A., Moradi, A., & Gill, P.
Affiliations
  • Tarbiat Modares University (IR)
  • University of Tehran (IR)
Corresponding author
Ranjbar, Bijan
ORCID
Venue
Photochemical & Photobiological Sciences
Publisher
Springer Science and Business Media LLC
Published
2010-03
Volume
9
Issue
3
Pages
376-383
ISSN
  • 1474-905X (ISSN-L)
  • 1474-9092
DOI
10.1039/b9pp00161a
OpenAlex
W2081654454
Cited by
18
References
0
Citations by year
2025: 1 · 2024: 1 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 1 · 2017: 1 · 2016: 2 · 2014: 1 · 2013: 1 · 2012: 2
FWCI
1.04
Type
journal article
Language
en
Open access
closed
Licence
Locations
  • Photochemical & Photobiological Sciences (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › bioluminescence and chemiluminescence research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
firefly luciferase, protein stability, Photinus pyralis, luciferase mutants, flexible loop, secondary structure, chemical denaturation, intrinsic fluorescence, extrinsic fluorescence, circular dichroism, differential scanning calorimetry
MeSH terms
Animals, Circular Dichroism, Mutation, Protein Denaturation, Urea, Gene Expression, Fireflies, Luciferases, Firefly, Luminescence, Protein Stability

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