2JI2

X-ray structure of E114A mutant of superoxide reductase from Desulfoarculus baarsii in the native, reduced form

2JI2 の概要

• エントリーDOI: 10.2210/pdb2ji2/pdb
• 関連するPDBエントリー: 1VZG 1VZH 1VZI 2JI1 2JI3
• 分子名称: Desulfoferrodoxin, FE (III) ION, NITRATE ION, ... (6 entities in total)
• 機能のキーワード: oxidoreductase, raman spectroscopy, superoxide reductase, intermediate trapping, microspectrophotometry, detoxification, electron transport, iron, transport, redox states, metal-binding
• 由来する生物種: Desulfarculus baarsii
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 57328.54

構造登録者

Katona, G.,Carpentier, P.,Niviere, V.,Amara, P.,Adam, V.,Ohana, J.,Tsanov, N.,Bourgeois, D. (登録日: 2007-02-24, 公開日: 2007-05-01, 最終更新日: 2023-12-13)

主引用文献

Katona, G.,Carpentier, P.,Niviere, V.,Amara, P.,Adam, V.,Ohana, J.,Tsanov, N.,Bourgeois, D.
Raman-assisted crystallography reveals end-on peroxide intermediates in a nonheme iron enzyme.
Science, 316:449-453, 2007

PubMed Abstract: Iron-peroxide intermediates are central in the reaction cycle of many iron-containing biomolecules. We trapped iron(III)-(hydro)peroxo species in crystals of superoxide reductase (SOR), a nonheme mononuclear iron enzyme that scavenges superoxide radicals. X-ray diffraction data at 1.95 angstrom resolution and Raman spectra recorded in crystallo revealed iron-(hydro)peroxo intermediates with the (hydro)peroxo group bound end-on. The dynamic SOR active site promotes the formation of transient hydrogen bond networks, which presumably assist the cleavage of the iron-oxygen bond in order to release the reaction product, hydrogen peroxide.

PubMed: 17446401
DOI: 10.1126/science.1138885

実験手法

X-RAY DIFFRACTION (1.7 Å)