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2J19

Ferrous Chloroperoxidase (high dose data set)

Summary for 2J19
Entry DOI10.2210/pdb2j19/pdb
Related1CPO 2CIV 2CIW 2CIX 2CIY 2CIZ 2CJ0 2CJ1 2CJ2 2CPO 2J18
Related PRD IDPRD_900111
DescriptorCHLOROPEROXIDASE, 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 Keywordspyrrolidone carboxylic acid, manganese, peroxidase, glycoprotein, metal-binding, oxidoreductase, iron, heme, chloride
Biological sourceCALDARIOMYCES FUMAGO
Total number of polymer chains1
Total formula weight36853.87
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 citationBeitlich, 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: 17211068
DOI: 10.1107/S0909049506049806
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.75 Å)
Structure validation

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