8qm3

formaldehyde-inhibited [FeFe]-hydrogenase I from Clostridium pasteurianum (CpI)

spinqualitylabelsall models 8qm3, resolution 1.53Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8qm3 is a 2 chain structure with sequence from Clostridium pasteurianum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.53Å Ligands: 402, CL, FES, FOR, GOL, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PHF1_CLOPA Publication Abstract from PubMed [FeFe]-hydrogenases are efficient H(2) converting biocatalysts that are inhibited by formaldehyde (HCHO). The molecular mechanism of this inhibition has so far not been experimentally solved. Here, we obtained high-resolution crystal structures of the HCHO-treated [FeFe]-hydrogenase CpI from Clostridium pasteurianum, showing HCHO reacts with the secondary amine base of the catalytic cofactor and the cysteine C299 of the proton transfer pathway which both are very important for catalytic turnover. Kinetic assays via protein film electrochemistry show the CpI variant C299D is significantly less inhibited by HCHO, corroborating the structural results. By combining our data from protein crystallography, site-directed mutagenesis and protein film electrochemistry, a reaction mechanism involving the cofactor's amine base, the thiol group of C299 and HCHO can be deduced. In addition to the specific case of [FeFe]-hydrogenases, our study provides additional insights into the reactions between HCHO and protein molecules. Insights into the Molecular Mechanism of Formaldehyde Inhibition of [FeFe]-Hydrogenases.,Duan J, Veliju A, Lampret O, Liu L, Yadav S, Apfel UP, Armstrong FA, Hemschemeier A, Hofmann E J Am Chem Soc. 2023 Dec 6;145(48):26068-26074. doi: 10.1021/jacs.3c07800. Epub , 2023 Nov 20. PMID:37983562 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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