7t30

Structure of electron bifurcating Ni-Fe hydrogenase complex HydABCSL in FMN/NAD(H) bound state

spinqualitylabelsall models 7t30, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7t30 is a 10 chain structure with sequence from Acetomicrobium mobile. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3Å Ligands: 3NI, FCO, FES, FMN, NAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function I4BYB4_ACEMN Publication Abstract from PubMed Electron bifurcation enables thermodynamically unfavorable biochemical reactions. Four groups of bifurcating flavoenzyme are known and three use FAD to bifurcate. FeFe-HydABC hydrogenase represents the fourth group, but its bifurcation site is unknown. We report cryo-EM structures of the related NiFe-HydABCSL hydrogenase that reversibly oxidizes H(2) and couples endergonic reduction of ferredoxin with exergonic reduction of NAD. FMN surrounded by a unique arrangement of iron sulfur clusters forms the bifurcating center. NAD binds to FMN in HydB, and electrons from H(2) via HydA to a HydB [4Fe-4S] cluster enable the FMN to reduce NAD. Low-potential electron transfer from FMN to the HydC [2Fe-2S] cluster and subsequent reduction of a uniquely penta-coordinated HydB [2Fe-2S] cluster require conformational changes, leading to ferredoxin binding and reduction by a [4Fe-4S] cluster in HydB. This work clarifies the electron transfer pathways for a large group of hydrogenases underlying many essential functions in anaerobic microorganisms. Structure and electron transfer pathways of an electron-bifurcating NiFe-hydrogenase.,Feng X, Schut GJ, Haja DK, Adams MWW, Li H Sci Adv. 2022 Feb 25;8(8):eabm7546. doi: 10.1126/sciadv.abm7546. Epub 2022 Feb , 25. PMID:35213221 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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