6NSZ
X-ray reduced Catalase 3 from N.Crassa (0.526 MGy)
Summary for 6NSZ
| Entry DOI | 10.2210/pdb6nsz/pdb |
| Related | 4AJ9 6NSW 6NSY |
| Descriptor | Catalase-3, PROTOPORPHYRIN IX CONTAINING FE, ACETATE ION, ... (10 entities in total) |
| Functional Keywords | x-ray reduced, heme, catalase, oxidoreductase |
| Biological source | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
| Total number of polymer chains | 4 |
| Total formula weight | 322583.19 |
| Authors | Zarate-Romero, A.,Rudino-Pinera, E.,Stojanoff, V. (deposition date: 2019-01-27, release date: 2019-05-01, Last modification date: 2023-10-11) |
| Primary citation | Zarate-Romero, A.,Stojanoff, V.,Cohen, A.E.,Hansberg, W.,Rudino-Pinera, E. X-ray driven reduction of Cpd I of Catalase-3 from N. crassa reveals differential sensitivity of active sites and formation of ferrous state. Arch.Biochem.Biophys., 666:107-115, 2019 Cited by PubMed Abstract: Catalases are biotechnologically relevant enzymes because of their applications in food technology, bioremediation, and biomedicine. The dismutation of hydrogen peroxide occurs in two steps; in the first one, the enzyme forms an oxidized compound I (Cpd I) and in the second one, the enzyme is reduced to the ferric state. In this research work, we analyzed the reduction of Cpd I by X-ray radiation damage during diffraction experiments in crystals of CAT-3, a Large-Size Subunit Catalase (LSC) from Neurospora crassa. A Multi-Crystal Data collection Strategy was applied in order to obtain the Cpd I structure at a resolution of 2.2 Å; this intermediate was highly sensitive to X-ray and was easily reduced at very low deposited radiation dose, causing breakage of the Fe=O bond. The comparison of the structures showed reduced intermediates and also evidenced the differential sensitivity per monomer. The resting ferric state was reduced to the ferrous state, an intermediate without a previous report in LSC. The chemically obtained Cpd I and the X-ray reduced intermediates were identified by UV-visible microspectrometry coupled to data collection. The differential sensitivity and the formation of a ferrous state are discussed, emphasizing the importance of the correct interpretation in the oxidation state of the iron heme. PubMed: 30940570DOI: 10.1016/j.abb.2019.03.020 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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