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

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.

Automated summary

This study investigates the tungsten-containing formate dehydrogenase from Methylorubrum extroquens AM1 (FoDH1), which has the potential as a biocatalyst. The research reveals the three-dimensional structure, electrode-active sites, and electron transfer pathways of FoDH1 using structural biology and bioelectrochemistry methods.