ArticleProtein science : a publication of the Protein Society2008
Structure-function studies on the active site of the coelenterazine-dependent luciferase from Renilla.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 60 citations in OpenAlex.
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- Insights into the bioluminescence systems of three sea pens (Cnidaria: Anthozoa): from de novo transcriptome analyses to biochemical assays.Open biology · 2025Article
- Optogenetics with Atomic Precision─A Comprehensive Review of Optical Control of Protein Function through Genetic Code Expansion.Chemical reviews · 2025Review
- Analysis of Calcium-Sensing Receptor Signaling Using Dual Luciferase Assays.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Exploring the Potential of Arginine to Increase Coelenterazine-Renilla Luciferase Affinity and Enzyme Stability: Kinetic and Molecular Dynamics Studies.The protein journal · 2024Article
- Uncovering the role of sorbitol inBiochemistry and biophysics reports · 2024Article
- Genetic Encoding of a Photocaged Histidine for Light-Control of Protein Activity.Chembiochem : a European journal of chemical biology · 2023Article
- Chemically Acylated tRNAs are Functional in Zebrafish Embryos.Journal of the American Chemical Society · 2023Article
- Engineering the protein dynamics of an ancestral luciferase.Nature communications · 2021Article
- A putative chordate luciferase from a cosmopolitan tunicate indicates convergent bioluminescence evolution across phyla.Scientific reports · 2020Article
- Self-illumination of Carbon Dots by Bioluminescence Resonance Energy Transfer.Scientific reports · 2019Article
- Highly bright and stable NIR-BRET with blue-shifted coelenterazine derivatives for deep-tissue imaging of molecular eventsTheranostics · 2019Article
- Luciferase-Specific Coelenterazine Analogues for Optical Contamination-Free Bioassays.Scientific reports · 2017Article
- A puzzling homology: a brittle star using a putative cnidarian-type luciferase for bioluminescence.Open biology · 2017Article
- A Dual Luciferase Reporter System forFrontiers in cellular and infection microbiology · 2017Article
- Techniques for the Analysis of Protein-Protein Interactions in Vivo.Plant physiology · 2016Review
- Porcine SOX9 Gene Expression Is Influenced by an 18 bp Indel in the 5'-Untranslated Region.PloS one · 2015Article
- Origin of the proton-transfer step in the cofactor-free (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase: effect of the basicity of an active site His residue.The Journal of biological chemistry · 2014Article
- Functional replacement of two highly conserved tetraloops in the bacterial ribosome.Biochemistry · 2012Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Renilla luciferase (RLUC) is a versatile tool for gene expression assays and in vivo biosensor applications, but its catalytic mechanism remains to be elucidated. RLUC is evolutionarily related to the alpha/beta hydrolase family. Its closest known homologs are bacterial dehalogenases, raising the question of how a protein with a hydrolase fold can function as a decarboxylating oxygenase. Molecular docking simulations with the coelenterazine substrate against an RLUC homology model as well as a recently determined RLUC crystal structure were used to build hypotheses to identify functionally important residues, which were subsequently tested by site-directed mutagenesis, heterologous expression, and bioluminescence emission spectroscopy. The data highlighted two triads of residues that are critical for catalysis. The putative catalytic triad residues D120, E144, and H285 bear only limited resemblance to those found in the active site of aequorin, a coelenterazine-utilizing photoprotein, suggesting that the reaction scheme employed by RLUC differs substantially from the one established for aequorin. The role of H285 in catalysis was further supported by inhibition using diethylpyrocarbonate. Multiple substitutions of N53, W121, and P220--three other residues implicated in product binding in the homologous dehalogenase Sphingomonas LinB--also supported their involvement in catalysis. Together with luminescence spectra, our data lead us to propose that the conserved catalytic triad of RLUC is directly involved in the decarboxylation reaction of coelenterazine to produce bioluminescence, while the other active-site residues are used for binding of the substrate.
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