Multiple electron transfer pathways of tungsten-containing formate dehydrogenase in direct electron transfer-type bioelectrocatalysis
Multiple electron transfer pathways of tungsten-containing formate dehydrogenase in direct electron transfer-type bioelectrocatalysis
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直接电子传递型生物电催化中含钨甲酸脱氢酶的多电子传递途径
DOI：
10.1039/d2cc01541b
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发表时间：
2022
影响因子：
4.9
通讯作者：
O
中科院分区：
文献类型：
--
作者：
Yoshikawa;T; Makino;F; Miyata;T; Suzuki;Y; Tanaka;H; Namba;K; Kano;K; Sowa;K; Kitazumi;Y; Shirai;O
利用结构生物学和生物电化学方法研究了一种具有良好生物催化活性的二氧化碳/甲酸和烟碱腺嘌呤二核苷酸（NAD+）/NADH氧化还原对相互转化的含钨甲酸脱氢酶（FoDH 1）.据报道，FoDH 1是一种可以实现“直接电子转移（DET）型生物电催化”的酶。然而，它的三维结构，电极活性位点和电子转移（ET）途径仍然不清楚。ET途径进行了研究，使用结构信息，电极和酶之间的静电相互作用，以及底物的差异。发现FoDH 1有两个电极活性位点和多条ET通路。
Tungsten-containing formate dehydrogenase from Methylorubrum extroquens AM1 (FoDH1)—a promising biocatalyst for the interconversion of carbon dioxide/formate and nicotine adenine dinucleotide (NAD+)/NADH redox couples—was investigated using structural biology and bioelectrochemistry. FoDH1 is reported to be an enzyme that can realize “direct electron transfer (DET)-type bioelectrocatalysis.” However, its 3-D structure, electrode-active sites, and electron transfer (ET) pathways remain unclear. The ET pathways were investigated using structural information, electrostatic interactions between the electrode and the enzyme, and the differences in the substrates. Two electrode-active sites and multiple ET pathways in FoDH1 were discovered.