Tryptophan-accelerated electron flow across a protein-protein interface

We report a new metallolabeled blue copper protein, Re126W122Cu(I) Pseudomonas aeruginosa azurin, which has three redox sites at well-defined distances in the protein fold: Re(I)(CO)3(4,7-dimethyl-1,10-phenanthroline) covalently bound at H126, a Cu center, and an indole side chain W122 situated betw...

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Bibliographic Details

Published in:	Journal of the American Chemical Society Vol. 135; no. 41; p. 15515
Main Authors:	Takematsu, Kana, Williamson, Heather, Blanco-Rodríguez, Ana María, Sokolová, Lucie, Nikolovski, Pavle, Kaiser, Jens T, Towrie, Michael, Clark, Ian P, Vlček, Jr, Antonín, Winkler, Jay R, Gray, Harry B
Format:	Journal Article
Language:	English
Published:	United States 16.10.2013
Subjects:	Azurin - chemistry Azurin - genetics Azurin - metabolism Electron Transport Electrons Models, Molecular Protein Folding Protein Interaction Domains and Motifs Pseudomonas aeruginosa - chemistry Pseudomonas aeruginosa - metabolism Rhenium - chemistry Rhenium - metabolism Tryptophan - chemistry Tryptophan - metabolism
ISSN:	1520-5126, 1520-5126
Online Access:	Get more information
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