2I7O

Structure of Re(4,7-dimethyl-phen)(Thr124His)(Lys122Trp)(His83Gln)AzCu(II), a Rhenium modified Azurin mutant

2I7O の概要

• エントリーDOI: 10.2210/pdb2i7o/pdb
• 関連するPDBエントリー: 1BEX
• 分子名称: Azurin, COPPER (II) ION, (1,10 PHENANTHROLINE)-(TRI-CARBON MONOXIDE) RHENIUM (I), ... (4 entities in total)
• 機能のキーワード: azurin, rhenium, elecron transfer, tryptophan, 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: 14586.91

構造登録者

Sudhamsu, J.,Crane, B.R. (登録日: 2006-08-31, 公開日: 2007-08-14, 最終更新日: 2024-11-06)

主引用文献

Shih, C.,Museth, A.K.,Abrahamsson, M.,Blanco-Rodriguez, A.M.,Di Bilio, A.J.,Sudhamsu, J.,Crane, B.R.,Ronayne, K.L.,Towrie, M.,Vlcek, A.,Richards, J.H.,Winkler, J.R.,Gray, H.B.
Tryptophan-accelerated electron flow through proteins.
Science, 320:1760-1762, 2008

PubMed Abstract: Energy flow in biological structures often requires submillisecond charge transport over long molecular distances. Kinetics modeling suggests that charge-transfer rates can be greatly enhanced by multistep electron tunneling in which redox-active amino acid side chains act as intermediate donors or acceptors. We report transient optical and infrared spectroscopic experiments that quantify the extent to which an intervening tryptophan residue can facilitate electron transfer between distant metal redox centers in a mutant Pseudomonas aeruginosa azurin. Cu(I) oxidation by a photoexcited Re(I)-diimine at position 124 on a histidine(124)-glycine(123)-tryptophan(122)-methionine(121) beta strand occurs in a few nanoseconds, fully two orders of magnitude faster than documented for single-step electron tunneling at a 19 angstrom donor-acceptor distance.

PubMed: 18583608
DOI: 10.1126/science.1158241

実験手法

X-RAY DIFFRACTION (1.5 Å)