2J5M
Structure of Chloroperoxidase Compound 0
Summary for 2J5M
| Entry DOI | 10.2210/pdb2j5m/pdb |
| Related PRD ID | PRD_900111 |
| Descriptor | CHLOROPEROXIDASE, 1,2-ETHANEDIOL, ACETATE ION, ... (12 entities in total) |
| Functional Keywords | oxidoreductase, pyrrolidone carboxylic acid, glycoprotein, metal-binding, peroxidase |
| Biological source | LEPTOXYPHIUM FUMAGO |
| Total number of polymer chains | 1 |
| Total formula weight | 36949.44 |
| Authors | Kuhnel, K.,Derat, E.,Terner, J.,Shaik, S.,Schlichting, I. (deposition date: 2006-09-18, release date: 2006-12-06, Last modification date: 2024-11-13) |
| Primary citation | Kuhnel, K.,Derat, E.,Terner, J.,Shaik, S.,Schlichting, I. Structure and Quantum Chemical Characterization of Chloroperoxidase Compound 0, a Common Reaction Intermediate of Diverse Heme Enzymes. Proc.Natl.Acad.Sci.USA, 104:99-, 2007 Cited by PubMed Abstract: We have determined the crystal structure of the chloroperoxidase (CPO) hydroperoxo reaction intermediate (CPO compound 0) at 1.75-A resolution. The intermediate was generated through controlled photoreduction of the CPO oxygen complex during x-ray data collection, which was monitored by recording of the crystal absorption spectra. Initially, the peroxo-anion species was formed and then protonated to yield compound 0. Quantum chemical calculations indicate that the peroxo-anion species is not stable and collapses instantaneously to compound 0. Compound 0 is present in the ferric low-spin doublet ground state and is characterized by a long O O bond length of 1.5 A and a Fe O bond distance of 1.8 A, which is also observed in the crystal structure. PubMed: 17190816DOI: 10.1073/PNAS.0606285103 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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