Çakar M Mervan, Mangas-Sanchez Juan, Birmingham William R, Turner Nicholas J, Binay Barış
a Department of Chemistry , Gebze Technical University , Gebze , Kocaeli , Turkey.
b School of Chemistry & MIB , University of Manchester , Manchester , UK.
Prep Biochem Biotechnol. 2018 Apr 21;48(4):327-334. doi: 10.1080/10826068.2018.1446150. Epub 2018 Mar 30.
Over the next decades, with the growing concern of rising atmospheric carbon dioxide (CO) levels, the importance of investigating new approaches for its reduction becomes crucial. Reclamation of CO for conversion into biofuels represents an alternative and attractive production method that has been studied in recent years, now with enzymatic methods gaining more attention. Formate dehydrogenases (FDHs) are NAD(P)H-dependent oxidoreductases that catalyze the conversion of formate into CO and have been extensively used for cofactor recycling in chemoenzymatic processes. A new FDH from Clostridium ljungdahlii (ClFDH) has been recently shown to possess activity in the reverse reaction: the mineralization of CO into formate. In this study, we show the successful homologous expression of ClFDH in Escherichia coli. Biochemical and kinetic characterization of the enzyme revealed that this homologue also demonstrates activity toward CO reduction. Structural analysis of the enzyme through homology modeling is also presented.
在接下来的几十年里，随着人们对大气中二氧化碳（CO）水平上升的日益关注，研究减少二氧化碳的新方法变得至关重要。回收二氧化碳以转化为生物燃料是一种近年来已被研究的替代且有吸引力的生产方法，目前酶法正受到更多关注。甲酸脱氢酶（FDHs）是依赖烟酰胺腺嘌呤二核苷酸（磷酸）（NAD(P)H）的氧化还原酶，可催化甲酸转化为二氧化碳，并已广泛用于化学酶促过程中的辅因子循环。最近发现，来自尤氏梭菌的一种新型甲酸脱氢酶（ClFDH）在逆反应中具有活性：将二氧化碳矿化为甲酸。在本研究中，我们展示了ClFDH在大肠杆菌中的成功同源表达。对该酶的生化和动力学表征表明，这种同源物也表现出对二氧化碳还原的活性。本文还通过同源建模对该酶进行了结构分析。
