Tryptophan-Accelerated Electron Flow Across a Protein–Protein Interface

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: ReI(CO)3(4,7-dimethyl-1,10-phenanthroline) covalently bound at H126, a Cu center, and an indole side chain W122 situated between...

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Veröffentlicht in:Journal of the American Chemical Society 2013-10, Vol.135 (41), p.15515-15525
Hauptverfasser: Takematsu, Kana, Williamson, Heather, Blanco-Rodríguez, Ana María, Sokolová, Lucie, Nikolovski, Pavle, Kaiser, Jens T, Towrie, Michael, Clark, Ian P, Vlček, Antonín, Winkler, Jay R, Gray, Harry B
Format: Artikel
Sprache:eng
Schlagworte:
Azurin - chemistry
Azurin - genetics
Azurin - metabolism
copper
crystal structure
Electron Transport
Electrons
mass spectrometry
Models, Molecular
oxidation
Protein Folding
Protein Interaction Domains and Motifs
protein-protein interactions
Pseudomonas aeruginosa
Pseudomonas aeruginosa - chemistry
Pseudomonas aeruginosa - metabolism
Rhenium - chemistry
Rhenium - metabolism
spectral analysis
tryptophan
Tryptophan - chemistry
Tryptophan - metabolism
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Zusammenfassung: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: ReI(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 CuI oxidation (
ISSN:0002-7863
1520-5126
1520-5126
DOI:10.1021/ja406830d