Multiple electron transfer pathways of tungsten-containing formate dehydrogenase in direct electron transfer-type bioelectrocatalysis.

Tatsushi Yoshikawa, Fumiaki Makino, Tomoko Miyata, Yohei Suzuki, Hideaki Tanaka, Keiichi Namba, Kenji Kano, Keisei Sowa, Yuki Kitazumi, Osamu Shirai

Chemical communications (Cambridge, England) 2022 Jun 01

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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.

Citation

Tatsushi Yoshikawa, Fumiaki Makino, Tomoko Miyata, Yohei Suzuki, Hideaki Tanaka, Keiichi Namba, Kenji Kano, Keisei Sowa, Yuki Kitazumi, Osamu Shirai. Multiple electron transfer pathways of tungsten-containing formate dehydrogenase in direct electron transfer-type bioelectrocatalysis. Chemical communications (Cambridge, England). 2022 Jun 01;58(45):6478-6481