Ontology highlight
ABSTRACT:
SUBMITTER: Keisei Sowa
PROVIDER: EMPIAR-11286 | biostudies-other |
REPOSITORIES: biostudies-other
Yoshikawa Tatsushi T Makino Fumiaki F Miyata Tomoko T Suzuki Yohei Y Tanaka Hideaki H Namba Keiichi K Kano Kenji K Sowa Keisei K Kitazumi Yuki Y Shirai Osamu O
Chemical communications (Cambridge, England) 20220601 45
Tungsten-containing formate dehydrogenase from <i>Methylorubrum extroquens</i> AM1 (FoDH1)-a promising biocatalyst for the interconversion of carbon dioxide/formate and nicotine adenine dinucleotide (NAD<sup>+</sup>)/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 ...[more]