2FJS

Crystal Structure of Anaerobically Reduced Wild Type Nitrite Reductase from A. faecalis

2FJS の概要

• エントリーDOI: 10.2210/pdb2fjs/pdb
• 関連するPDBエントリー: 1AQ8 1AS7 1AS8
• 分子名称: Copper-containing nitrite reductase, COPPER (I) ION, COPPER (II) ION, ... (6 entities in total)
• 機能のキーワード: blue copper protein, cupredoxin fold, oxidoreductase
• 由来する生物種: Alcaligenes faecalis
• 細胞内の位置: Periplasm: P38501
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 110360.26

構造登録者

Tocheva, E.I.,Murphy, M.E.P. (登録日: 2006-01-03, 公開日: 2006-11-21, 最終更新日: 2023-08-30)

主引用文献

Wijma, H.J.,MacPherson, I.,Farver, O.,Tocheva, E.I.,Pecht, I.,Verbeet, M.P.,Murphy, M.E.P.,Canters, G.W.
Effect of the methionine ligand on the reorganization energy of the type-1 copper site of nitrite reductase.
J.Am.Chem.Soc., 129:519-525, 2007

PubMed Abstract: Copper-containing nitrite reductase harbors a type-1 and a type-2 Cu site. The former acts as the electron acceptor site of the enzyme, and the latter is the site of catalytic action. The effect of the methionine ligand on the reorganization energy of the type-1 site was explored by studying the electron-transfer kinetics between NiR (wild type (wt) and the variants Met150Gly and Met150Thr) with Fe(II)EDTA and Fe(II)HEDTA. The mutations increased the reorganization energy by 0.3 eV (30 kJ mol-1). A similar increase was found from pulse radiolysis experiments on the wt NIR and three variants (Met150Gly, Met150His, and Met150Thr). Binding of the nearby Met62 to the type-1 Cu site in Met150Gly (under influence of an allosteric effector) lowered the reorganization energy back to approximately the wt value. According to XRD data the structure of the reduced type-1 site in Met150Gly NiR in the presence of an allosteric effector is similar to that in the reduced wt NiR (solved to 1.85 A), compatible with the similarity in reorganization energy.

PubMed: 17227014
DOI: 10.1021/ja064763j

実験手法

X-RAY DIFFRACTION (1.85 Å)