4AJ9

Catalase 3 from Neurospora crassa

Summary for 4AJ9

• Entry DOI: 10.2210/pdb4aj9/pdb
• Descriptor: CATALASE-3, PROTOPORPHYRIN IX CONTAINING FE, ACETATE ION, ... (5 entities in total)
• Functional Keywords: oxidoreductase, peroxidase
• Biological source: NEUROSPORA CRASSA
• Total number of polymer chains: 4
• Total formula weight: 311225.82

Authors

Zarate-Romero, A.,Rudino-Pinera, E. (deposition date: 2012-02-16, release date: 2013-03-06, Last modification date: 2023-12-20)

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

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: 30940570
DOI: 10.1016/j.abb.2019.03.020

Experimental method

X-RAY DIFFRACTION (1.85 Å)