A novel, NADH-dependent acrylate reductase in Vibrio harveyiстатья
Статья опубликована в высокорейтинговом журнале
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Дата последнего поиска статьи во внешних источниках: 13 июля 2022 г.
Аннотация:Bacteria coping with oxygen deficiency use alternative terminal electronacceptors for NADH regeneration, particularly fumarate. Fumarate is reduced by theFAD_binding_2 domain of cytoplasmic fumarate reductase in many bacteria. The variabilityof the primary structure of this domain in homologous proteins suggests the existenceof reducing activities with different specificities. Here, we produced and characterized onesuch protein encoded in the Vibrio harveyi genome (GenBank ID: AIV07243) and found itto be a specific NADH:acrylate oxidoreductase (ARD). This previously unknown enzyme isformed by the OYE-like, FMN_bind, and FAD_binding_2 domains and contains covalentlybound flavin mononucleotide (FMN) and noncovalently bound flavin adenine dinucleotide(FAD) and FMN in a ratio of 1:1:1. The covalently bound FMN is absolutely requiredfor activity and is attached by the specific flavin transferase, ApbE, to the FMN_bind domain.Quantitative reverse transcription PCR (RT-qPCR) and activity measurements indicateddramatic stimulation of ARD biosynthesis by acrylate in the V. harveyi cells grownaerobically. In contrast, the ard gene expression in the cells grown anaerobically withoutacrylate was higher than that in aerobic cultures and increased only 2-fold in the presenceof acrylate. These findings suggest that the principal role of ARD in Vibrio is energysavingdetoxification of acrylate coming from the environment.