Chemical studies on the chiral indanone derivatives as the inhibitor of Renilla luciferase
摘要:
The bioluminescence reaction of coelenterazine involves an oxidative process. To investigate the reaction mechanism, we synthesized three mechanism-based inhibitors with an indanone core structure. The inhibitors exhibited the competitive inhibition of the Renilla luciferase reaction. The (-)-4-benzyl-2-(4-hydroxybenzyl)-2-hydroxymethyl-6-(4-hydroxyphenyl)-indan-1-one showed the significant enantio-selectivity of the inhibition and its absolute configuration was assigned as the R-configuration. These inhibitors could be useful probes to study the catalytic environment in the coelenterazine-luciferase reaction. (C) 2001 Elsevier Science Ltd. All rights reserved.
作者:Richard R Hark、Diane B Hauze、Olga Petrovskaia、Madeleine M Joullié
DOI:10.1139/v01-143
日期:2001.11.1
Ninhydrin is an essential tool in the analysis of amino acids, peptides, and proteins, and the preferred re - agent for the detection of latent fingerprints on porous surfaces. The goal of this investigation was to prepare ninhydrinanalogs with enhanced chromogenic and fluorogenic properties. Target compounds included structures with extended conjugation and (or) with the presence of sulfur-containing
The bioluminescence reaction of coelenterazine involves an oxidative process. To investigate the reaction mechanism, we synthesized three mechanism-based inhibitors with an indanone core structure. The inhibitors exhibited the competitive inhibition of the Renilla luciferase reaction. The (-)-4-benzyl-2-(4-hydroxybenzyl)-2-hydroxymethyl-6-(4-hydroxyphenyl)-indan-1-one showed the significant enantio-selectivity of the inhibition and its absolute configuration was assigned as the R-configuration. These inhibitors could be useful probes to study the catalytic environment in the coelenterazine-luciferase reaction. (C) 2001 Elsevier Science Ltd. All rights reserved.
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