9vap | pdb_00009vap

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

spinqualitylabelsall models 9vap, resolution 2.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9vap is a 2 chain structure with sequence from Shewanella oneidensis MR-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.75Å Ligands: H2S, MGD, W Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Bioelectrocatalytic CO(2) reduction offers a sustainable route for CO(2) 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(2) reduction system is constructed, accumulating 2.88 +/- 0.03 mmol formate in 64 hours with a steady rate of 45.3 +/- 0.5 mumol h(-1) cm(-2) 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. An interfacial-intramolecular electron highway for accelerated electrocatalytic CO(2) reduction by an O(2)-tolerant formate dehydrogenase.,Liu W, Zhang P, Wang X, Zhang K, Yang W, Cui H, Liu J, Sun J, You C, Cui H, Zhu Z, Zhang L Nat Commun. 2026 Mar 3. doi: 10.1038/s41467-026-69827-w. PMID:41775696 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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