2J19
Ferrous Chloroperoxidase (high dose data set)
Summary for 2J19
| Entry DOI | 10.2210/pdb2j19/pdb |
| Related | 1CPO 2CIV 2CIW 2CIX 2CIY 2CIZ 2CJ0 2CJ1 2CJ2 2CPO 2J18 |
| Related PRD ID | PRD_900111 |
| Descriptor | CHLOROPEROXIDASE, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total) |
| Functional Keywords | pyrrolidone carboxylic acid, manganese, peroxidase, glycoprotein, metal-binding, oxidoreductase, iron, heme, chloride |
| Biological source | CALDARIOMYCES FUMAGO |
| Total number of polymer chains | 1 |
| Total formula weight | 36853.87 |
| Authors | Beitlich, T.,Kuhnel, K.,Schulze-Briese, C.,Shoeman, R.L.,Schlichting, I. (deposition date: 2006-08-09, release date: 2006-12-18, Last modification date: 2024-10-23) |
| Primary citation | Beitlich, T.,Kuhnel, K.,Schulze-Briese, C.,Shoeman, R.L.,Schlichting, I. Cryoradiolytic Reduction of Crystalline Heme Proteins: Analysis by Uv-Vis Spectroscopy and X-Ray Crystallography J.Synchrotron Radiat., 14:11-, 2007 Cited by PubMed Abstract: The X-ray crystallographic analysis of redox-active systems may be complicated by photoreduction. Although radiolytic reduction by the probing X-ray beam may be exploited to generate otherwise short-lived reaction intermediates of metalloproteins, it is generally an undesired feature. Here, the X-ray-induced reduction of the three heme proteins myoglobin, cytochrome P450cam and chloroperoxidase has been followed by on-line UV-Vis absorption spectroscopy. All three systems showed a very rapid reduction of the heme iron. In chloroperoxidase the change of the ionization state from ferric to ferrous heme is associated with a movement of the heme-coordinating water molecule. The influence of the energy of the incident X-ray photons and of the presence of scavengers on the apparent reduction rate of ferric myoglobin crystals was analyzed. PubMed: 17211068DOI: 10.1107/S0909049506049806 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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