In:
Chemical Communications, Royal Society of Chemistry (RSC), Vol. 58, No. 45 ( 2022), p. 6478-6481
Abstract:
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.
Type of Medium:
Online Resource
ISSN:
1359-7345
,
1364-548X
Language:
English
Publisher:
Royal Society of Chemistry (RSC)
Publication Date:
2022
detail.hit.zdb_id:
1472881-3
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