1JZE

Pseudomonas aeruginosa Azurin Ru(bpy)2(im)(His83)

1JZE の概要

• エントリーDOI: 10.2210/pdb1jze/pdb
• 関連するPDBエントリー: 1JZF 1JZG 1JZH 1JZI 1JZJ
• 分子名称: azurin, COPPER (II) ION, DELTA-BIS(2,2'-BIPYRIDINE)IMIDAZOLE RUTHENIUM (II), ... (5 entities in total)
• 機能のキーワード: blue-copper, electron transfer, ruthenium, electron transport
• 由来する生物種: Pseudomonas aeruginosa
• 細胞内の位置: Periplasm: P00282
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15049.91

構造登録者

Crane, B.R.,Di Bilio, A.J.,Winkler, J.R.,Gray, H.B. (登録日: 2001-09-16, 公開日: 2001-10-17, 最終更新日: 2024-10-30)

主引用文献

Crane, B.R.,Di Bilio, A.J.,Winkler, J.R.,Gray, H.B.
Electron tunneling in single crystals of Pseudomonas aeruginosa azurins.
J.Am.Chem.Soc., 123:11623-11631, 2001

PubMed Abstract: Rates of reduction of Os(III), Ru(III), and Re(I) by Cu(I) in His83-modified Pseudomonas aeruginosa azurins (M-Cu distance approximately 17 A) have been measured in single crystals, where protein conformation and surface solvation are precisely defined by high-resolution X-ray structure determinations: 1.7(8) x 10(6) s(-1) (298 K), 1.8(8) x 10(6) s(-1) (140 K), [Ru(bpy)2(im)(3+)-]; 3.0(15) x 10(6) s(-1) (298 K), [Ru(tpy)(bpy)(3+)-]; 3.0(15) x 10(6) s(-1) (298 K), [Ru(tpy)(phen)(3+)-]; 9.0(50) x 10(2) s(-1) (298 K), [Os(bpy)2(im)(3+)-]; 4.4(20) x 10(6) s(-1) (298 K), [Re(CO)3(phen)(+)] (bpy = 2,2'-bipyridine; im = imidazole; tpy = 2,2':6',2' '-terpyridine; phen = 1,10-phenanthroline). The time constants for electron tunneling in crystals are roughly the same as those measured in solution, indicating very similar protein structures in the two states. High-resolution structures of the oxidized (1.5 A) and reduced (1.4 A) states of Ru(II)(tpy)(phen)(His83)Az establish that very small changes in copper coordination accompany reduction but reveal a shorter axial interaction between copper and the Gly45 peptide carbonyl oxygen [2.6 A for Cu(II)] than had been recognized previously. Although Ru(bpy)2(im)(His83)Az is less solvated in the crystal, the reorganization energy for Cu(I) --> Ru(III) electron transfer falls in the range (0.6-0.8 eV) determined experimentally for the reaction in solution. Our work suggests that outer-sphere protein reorganization is the dominant activation component required for electron tunneling.

PubMed: 11716717
DOI: 10.1021/ja0115870

実験手法

X-RAY DIFFRACTION (1.6 Å)