8a5e | pdb_00008a5e

Cryo-EM structure of the electron bifurcating Fe-Fe hydrogenase HydABC complex from Acetobacterium woodii in the reduced state

spinqualitylabelsall models 8a5e, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8a5e is a 4 chain structure with sequence from Acetobacterium woodii DSM 1030. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.4Å Ligands: FES, FMN, HC1, NAI, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H6LFG4_ACEWD Publication Abstract from PubMed Electron bifurcation is a fundamental energy coupling mechanism widespread in microorganisms that thrive under anoxic conditions. These organisms employ hydrogen to reduce CO(2), but the molecular mechanisms have remained enigmatic. The key enzyme responsible for powering these thermodynamically challenging reactions is the electron-bifurcating [FeFe]-hydrogenase HydABC that reduces low-potential ferredoxins (Fd) by oxidizing hydrogen gas (H(2)). By combining single-particle cryo-electron microscopy (cryoEM) under catalytic turnover conditions with site-directed mutagenesis experiments, functional studies, infrared spectroscopy, and molecular simulations, we show that HydABC from the acetogenic bacteria Acetobacterium woodii and Thermoanaerobacter kivui employ a single flavin mononucleotide (FMN) cofactor to establish electron transfer pathways to the NAD(P)(+) and Fd reduction sites by a mechanism that is fundamentally different from classical flavin-based electron bifurcation enzymes. By modulation of the NAD(P)(+) binding affinity via reduction of a nearby iron-sulfur cluster, HydABC switches between the exergonic NAD(P)(+) reduction and endergonic Fd reduction modes. Our combined findings suggest that the conformational dynamics establish a redox-driven kinetic gate that prevents the backflow of the electrons from the Fd reduction branch toward the FMN site, providing a basis for understanding general mechanistic principles of electron-bifurcating hydrogenases. Molecular Basis of the Electron Bifurcation Mechanism in the [FeFe]-Hydrogenase Complex HydABC.,Katsyv A, Kumar A, Saura P, Poverlein MC, Freibert SA, T Stripp S, Jain S, Gamiz-Hernandez AP, Kaila VRI, Muller V, Schuller JM J Am Chem Soc. 2023 Mar 15;145(10):5696-5709. doi: 10.1021/jacs.2c11683. Epub , 2023 Feb 22. PMID:36811855 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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