Published in

American Chemical Society, Journal of the American Chemical Society, 41(135), p. 15515-15525, 2013

DOI: 10.1021/ja406830d

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Tryptophan-Accelerated Electron Flow Across a Protein−Protein Interface

This paper is available in a repository.
This paper is available in a repository.

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Abstract

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 between the Re and Cu sites (Re-W122(indole) = 13.1 Å, dmp-W122(indole) = 10.0 Å, Re-Cu = 25.6 Å). Near-UV excitation of the Re chromophore leads to prompt Cu^I oxidation (