Imidazole-assisted Catalysis of Luminescence Reaction in Blue Fluorescent Protein from the Photoprotein Aequorin.
From: Yokohama Research Center, Chisso Corporation, 5-1 Okawa, Kanazawa-ku, Yokohama 236-8605, Japan. sinouye@chisso.co.jp
Biochemical and biophysical research communications
- Publish Date: Mar 2007
- ISSN: 0006-291X
- Volume: 354
- Issue: 3
- Pages: 650-5
- Medium: Print
- Language: English
- Citation (JAMA): Inouye Satoshi, Sasaki Satoko, et al. Imidazole-assisted Catalysis of Luminescence Reaction in Blue Fluorescent Protein from the Photoprotein Aequorin.. Biochem. Biophys. Res. Commun. Mar 2007;354:650-5
Abstract
Blue fluorescent protein from the calcium-binding photoprotein aequorin (BFP-aq) is a dissociable complex of Ca(2+)-bound apoaequorin and coelenteramide, and is identified as a luciferase that catalyzes the oxidation of coelenterazine by molecular oxygen to emit light. Based on the chemical luminescence of coelenterazine oxidation by an acid-base mechanism, we found that the luminescence activity of BFP-aq was stimulated by imidazole at concentrations of 30-300mM with coelenterazine and its analogues. The kinetic analyses indicate that imidazole has no effect on the binding affinity of coelenterazine to BFP-aq and may act as a catalytic base, accepting a proton from the -NH- group of coelenterazine and stimulating luminescence activity.
Mesh Headings (Keywords): Aequorin, Amides, Binding Sites, Calcium, Catalysis, Imidazoles, Kinetics, Luciferases, Luminescent Agents, Luminescent Proteins, Osmolar Concentration, Oxidation-Reduction, Oxygen, Protons, Pyrazines, Spectrometry, Fluorescence
Check for Full Text / PubMed Unique Identifier (PMID): 17254548
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