1H55
STRUCTURE OF HORSERADISH PEROXIDASE C1A COMPOUND II
Summary for 1H55
| Entry DOI | 10.2210/pdb1h55/pdb |
| Related | 1ATJ 1H57 1H58 1HCH 2ATJ 3ATJ 6ATJ 7ATJ |
| Descriptor | PEROXIDASE C1A, PROTOPORPHYRIN IX CONTAINING FE, ACETATE ION, ... (6 entities in total) |
| Functional Keywords | oxidoreductase, peroxidase, horseradish, catalytic intermediate, compound ii |
| Biological source | ARMORACIA RUSTICANA (HORSERADISH) |
| Cellular location | Secreted (Probable): P00433 |
| Total number of polymer chains | 1 |
| Total formula weight | 34719.83 |
| Authors | Berglund, G.I.,Carlsson, G.H.,Hajdu, J.,Smith, A.T.,Szoke, H.,Henriksen, A. (deposition date: 2001-05-18, release date: 2002-06-18, Last modification date: 2024-10-16) |
| Primary citation | Berglund, G.I.,Carlsson, G.H.,Smith, A.T.,Szoke, H.,Henriksen, A.,Hajdu, J. The Catalytic Pathway of Horseradish Peroxidase at High Resolution Nature, 417:463-, 2002 Cited by PubMed Abstract: A molecular description of oxygen and peroxide activation in biological systems is difficult, because electrons liberated during X-ray data collection reduce the active centres of redox enzymes catalysing these reactions. Here we describe an effective strategy to obtain crystal structures for high-valency redox intermediates and present a three-dimensional movie of the X-ray-driven catalytic reduction of a bound dioxygen species in horseradish peroxidase (HRP). We also describe separate experiments in which high-resolution structures could be obtained for all five oxidation states of HRP, showing such structures with preserved redox states for the first time. PubMed: 12024218DOI: 10.1038/417463A PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.61 Å) |
Structure validation
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