1DCC
2.2 ANGSTROM STRUCTURE OF OXYPEROXIDASE: A MODEL FOR THE ENZYME:PEROXIDE COMPLEX
Summary for 1DCC
| Entry DOI | 10.2210/pdb1dcc/pdb |
| Related | 1CCP 3CCP |
| Descriptor | CYTOCHROME C PEROXIDASE, OXYGEN MOLECULE, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total) |
| Functional Keywords | oxidoreductase(h2o2(a)) |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Mitochondrion matrix: P00431 |
| Total number of polymer chains | 1 |
| Total formula weight | 34379.06 |
| Authors | Miller, M.A.,Shaw, A.,Kraut, J. (deposition date: 1994-06-01, release date: 1994-08-31, Last modification date: 2024-02-07) |
| Primary citation | Miller, M.A.,Shaw, A.,Kraut, J. 2.2 A structure of oxy-peroxidase as a model for the transient enzyme: peroxide complex. Nat.Struct.Biol., 1:524-531, 1994 Cited by PubMed Abstract: The Fe+3-OOH complex of peroxidases has a very short half life, and its structure cannot be determined by conventional methods. The Fe+2-O2 complex provides a useful structural model for this intermediate, as it differs by only one electron and one proton from the transient Fe+3-OOH complex. We therefore determined the crystal structure of the Fe+2-O2 complex formed by a yeast cytochrome c peroxidase mutant with Trp 191 replaced by Phe. The refined structure shows that dioxygen can form a hydrogen bond with the conserved distal His residue, but not with the conserved distal Arg residue. When the transient Fe+3-OOH complex is modelled in a similar orientation, the active site of peroxidase appears to be optimized for catalysing proton transfer between the vicinal oxygen atoms of the peroxy-anion. PubMed: 7664080DOI: 10.1038/nsb0894-524 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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