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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Vydané v:	Journal of the American Chemical Society Ročník 135; číslo 41; s. 15515
Hlavní autori:	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
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	United States 16.10.2013
Predmet:	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
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