6NSW

X-ray reduced Catalase 3 From N.Crassa in Cpd I state (0.135 MGy)

6NSW の概要

• エントリーDOI: 10.2210/pdb6nsw/pdb
• 関連するPDBエントリー: 4AJ9
• 分子名称: Catalase-3, TETRAETHYLENE GLYCOL, PROTOPORPHYRIN IX CONTAINING FE, ... (11 entities in total)
• 機能のキーワード: x-ray reduced, heme, compound i, oxidoreductase
• 由来する生物種: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 322450.94

構造登録者

Zarate-Romero, A.,Rudino-Pinera, E.,Stojanoff, V. (登録日: 2019-01-25, 公開日: 2019-05-01, 最終更新日: 2023-10-11)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.099 Å)