3PZA
Fully Reduced (All-ferrous) Pyrococcus rubrerythrin after a 10 second exposure to peroxide.
Summary for 3PZA
| Entry DOI | 10.2210/pdb3pza/pdb |
| Descriptor | Rubrerythrin, HYDROGEN PEROXIDE, FE (II) ION, ... (4 entities in total) |
| Functional Keywords | rubrerythrin, oxidoreductase |
| Biological source | Pyrococcus furiosus |
| Total number of polymer chains | 2 |
| Total formula weight | 39199.78 |
| Authors | Dillard, B.D.,Demick, J.M.,Adams, M.W.,Lanzilotta, W.N. (deposition date: 2010-12-14, release date: 2011-06-22, Last modification date: 2024-02-21) |
| Primary citation | Dillard, B.D.,Demick, J.M.,Adams, M.W.,Lanzilotta, W.N. A cryo-crystallographic time course for peroxide reduction by rubrerythrin from Pyrococcus furiosus. J.Biol.Inorg.Chem., 16:949-959, 2011 Cited by PubMed Abstract: High-resolution crystal structures of Pyrococcus furiosus rubrerythrin (PfRbr) in the resting (all-ferrous) state and at time points following exposure of the crystals to hydrogen peroxide are reported. This approach was possible because of the relativity slow turnover of PfRbr at room temperature. To this end, we were able to perform time-dependent peroxide treatment of the fully reduced enzyme, under strictly anaerobic conditions, in the crystalline state. In this work we demonstrate, for the first time, that turnover of a thermophilic rubrerythrin results in approximately 2-Å movement of one iron atom in the diiron site from a histidine to a carboxylate ligand. These results confirm that, despite the domain-swapped architecture, the hyperthermophilic rubrerythrins also utilize the classic combination of iron sites together with redox-dependent iron toggling to selectively reduce hydrogen peroxide over dioxygen. In addition, we have identified previously unobserved intermediates in the reaction cycle and observed structural changes that may explain the enzyme precipitation observed for the all-iron form of PfRbr upon oxidation to the all-ferric state. PubMed: 21647777DOI: 10.1007/s00775-011-0795-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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