Tryptophan-accelerated electron flow through proteins

被引:361
作者
Shih, Crystal [2 ]
Museth, Anna Katrine [2 ]
Abrahamsson, Malin [2 ]
Blanco-Rodriguez, Ana Maria [3 ]
Di Bilio, Angel J. [2 ]
Sudhamsu, Jawahar [1 ]
Crane, Brian R. [1 ]
Ronayne, Kate L. [4 ]
Towrie, Mike [4 ]
Vlcek, Antonin, Jr. [3 ]
Richards, John H. [2 ]
Winkler, Jay R. [2 ]
Gray, Harry B. [2 ]
机构
[1] Cornell Univ, Dept Chem & Chem Biol, Ithaca, NY 14853 USA
[2] CALTECH, Beckman Inst, Pasadena, CA 91125 USA
[3] Queen Mary Univ London, Sch Biol & Chem Sci, London E1 4NS, England
[4] STFC Rutherford Appleton Lab, Cent Laser Facil, Didcot OX11 0QX, Oxon, England
基金
美国国家科学基金会;
关键词
D O I
10.1126/science.1158241
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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-1 oxidation by a photoexcited Re-1- 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.
引用
收藏
页码:1760 / 1762
页数:3
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