6v59

Crystal structure of the diheme peroxidase BthA Y463M variant from Burkholderia thailandensis E264

spinqualitylabelsall models 6v59, resolution 1.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.593Å Ligands: CL, GOL, HEC, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed BthA is a diheme enzyme that is a member of the bacterial cytochrome c peroxidase superfamily, capable of generating a highly unusual Fe(IV)Fe(IV) horizontal lineO oxidation state, known to be responsible for long-range oxidative chemistry in the enzyme MauG. Here, we show that installing a canonical Met ligand in lieu of the Tyr found at the heme of MauG associated with electron transfer, results in a construct that yields an unusually stable Fe(IV) horizontal lineO porphyrin at the peroxidatic heme. This state is spontaneously formed at ambient conditions using either molecular O2 or H2O2. The resulting data illustrate how a ferryl iron, with unforeseen stability, may be achieved in biology. A Stable Ferryl Porphyrin at the Active Site of Y463M BthA.,Rizzolo K, Weitz AC, Cohen SE, Drennan CL, Hendrich MP, Elliott SJ J Am Chem Soc. 2020 Jul 1. doi: 10.1021/jacs.0c04023. PMID:32564595 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome c peroxidase 3D structures

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