9VAP

Cryo-EM structure of formate dehydrogenase from Shewanella oneidensis MR-1 (SoFdhAB)

Summary for 9VAP

• Entry DOI: 10.2210/pdb9vap/pdb
• EMDB information: 64903
• Descriptor: Formate dehydrogenase molybdopterin-binding subunit FdhA, 4Fe-4S dicluster domain-containing protein, 2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE, ... (6 entities in total)
• Functional Keywords: formate dehydrogenase, carbon dioxide reduction, tungsten (w)-dependent, oxidoreductase
• Biological source: Shewanella oneidensis MR-1; More
• Total number of polymer chains: 2
• Total formula weight: 131865.10

Authors

Liu, W.,Zhang, L. (deposition date: 2025-06-03, release date: 2026-04-08)

Primary citation

Liu, W.,Zhang, P.,Wang, X.,Zhang, K.,Yang, W.,Cui, H.,Liu, J.,Sun, J.,You, C.,Cui, H.,Zhu, Z.,Zhang, L.
An interfacial-intramolecular electron highway for accelerated electrocatalytic CO 2 reduction by an O 2 -tolerant formate dehydrogenase.
Nat Commun, 2026

PubMed Abstract: Bioelectrocatalytic CO reduction offers a sustainable route for CO bioconversion, yet remains limited by interfacial-intramolecular electron transfer and oxygen sensitivity. Here, we mine a formate dehydrogenase from Shewanella oneidensis MR-1 (SoFdhAB) featuring completely oxygen tolerant and direct-electron-transfer (DET) electrocatalytic performances. Cryo-electron microscopy (Cryo-EM) analysis reveals an intramolecular electron highway comprising five [4Fe-4S] clusters, a regional face-face contact facilitating interfacial ET, and a unique oxygen resistance mechanism different from inactivation-activation. By acquiring a beneficial variant SoFdhAB-Y94S, a direct bioelectrocatalytic CO reduction system is constructed, accumulating 2.88 ± 0.03 mmol formate in 64 hours with a steady rate of 45.3 ± 0.5 μmol h cm and a Faradaic efficiency of 93.1 ± 5.2%. The merits of oxygen tolerance and efficient (electro)catalytic property endow SoFdhAB a robust enzyme adopted in potential application scenarios, and the inherent DET capability may inspire the interfacial engineering of other oxidoreductases.

PubMed: 41775696
DOI: 10.1038/s41467-026-69827-w

Experimental method

ELECTRON MICROSCOPY (2.75 Å)