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TitleMultiple electron transfer pathways of tungsten-containing formate dehydrogenase in direct electron transfer-type bioelectrocatalysis.
Journal, issue, pagesChem Commun (Camb), Vol. 58, Issue 45, Page 6478-6481, Year 2022
Publish dateJun 1, 2022
AuthorsTatsushi Yoshikawa / Fumiaki Makino / Tomoko Miyata / Yohei Suzuki / Hideaki Tanaka / Keiichi Namba / Kenji Kano / Keisei Sowa / Yuki Kitazumi / Osamu Shirai /
PubMed AbstractTungsten-containing formate dehydrogenase from AM1 (FoDH1)-a promising biocatalyst for the interconversion of carbon dioxide/formate and nicotine adenine dinucleotide (NAD)/NADH redox couples-was ...Tungsten-containing formate dehydrogenase from 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.
External linksChem Commun (Camb) / PubMed:35535582
MethodsEM (single particle)
Resolution2.19 Å
Structure data

32151

7vw6

EMDB-32151, PDB-7vw6:
Cryo-EM Structure of Formate Dehydrogenase 1 from Methylorubrum extorquens AM1
Method: EM (single particle) / Resolution: 2.19 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-MGD:
2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE

ChemComp-W:
Unknown entry

ChemComp-UNX:
Unknown entry

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

Source
  • methylorubrum extorquens am1 (bacteria)
KeywordsOXIDOREDUCTASE / Complex

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