6V59
Crystal structure of the diheme peroxidase BthA Y463M variant from Burkholderia thailandensis E264
Summary for 6V59
| Entry DOI | 10.2210/pdb6v59/pdb |
| Descriptor | Di-haem cytochrome c peroxidase family protein, HEME C, GLYCEROL, ... (6 entities in total) |
| Functional Keywords | heme, peroxidase, diheme, oxidoreductase, btha |
| Biological source | Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264) |
| Total number of polymer chains | 2 |
| Total formula weight | 106260.54 |
| Authors | Cohen, S.E.,Drennan, C.L. (deposition date: 2019-12-03, release date: 2020-07-08, Last modification date: 2024-10-30) |
| Primary citation | Rizzolo, K.,Weitz, A.C.,Cohen, S.E.,Drennan, C.L.,Hendrich, M.P.,Elliott, S.J. A Stable Ferryl Porphyrin at the Active Site of Y463M BthA. J.Am.Chem.Soc., 142:11978-11982, 2020 Cited by PubMed Abstract: 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)═O 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)═O porphyrin at the peroxidatic heme. This state is spontaneously formed at ambient conditions using either molecular O or HO. The resulting data illustrate how a ferryl iron, with unforeseen stability, may be achieved in biology. PubMed: 32564595DOI: 10.1021/jacs.0c04023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.593 Å) |
Structure validation
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