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| Description
| - We report a new metallolabeled blue copper protein, Re126W122CuI 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 (<50 ns), followed by slow back ET to regenerate CuI and ground-state ReI with biexponential kinetics, 220 ns and 6 μs. From spectroscopic measurements of kinetics and relative ET yields at different concentrations, it is likely that the photoinduced ET reactions occur in protein dimers, (Re126W122CuI)2 and that the forward ET is accelerated by intermolecular electron hopping through the interfacial tryptophan: *Re//<-W122<-CuI, where // denotes a proteinprotein interface. Solution mass spectrometry confirms a broad oligomer distribution with prevalent monomers and dimers, and the crystal structure of the CuII form shows two Re126W122CuII molecules oriented such that redox cofactors Re(dmp) and W122-indole on different protein molecules are located at the interface at much shorter intermolecular distances (Re-W122(indole) = 6.9 Å, dmp-W122(indole) = 3.5 Å, and Re- Cu = 14.0 Å) than within single protein folds. Whereas forward ET is accelerated by hopping through W122, BET is retarded by a space jump at the interface that lacks specific interactions or water molecules. These findings on interfacial electron hopping in (Re126W122CuI)2 shed new light on optimal redox-unit placements required for functional long-range charge separation in protein complexes.
- We report a new metallolabeled blue copper protein, Re126W122CuI 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 (<50 ns), followed by slow back ET to regenerate CuI and ground-state ReI with biexponential kinetics, 220 ns and 6 μs. From spectroscopic measurements of kinetics and relative ET yields at different concentrations, it is likely that the photoinduced ET reactions occur in protein dimers, (Re126W122CuI)2 and that the forward ET is accelerated by intermolecular electron hopping through the interfacial tryptophan: *Re//<-W122<-CuI, where // denotes a proteinprotein interface. Solution mass spectrometry confirms a broad oligomer distribution with prevalent monomers and dimers, and the crystal structure of the CuII form shows two Re126W122CuII molecules oriented such that redox cofactors Re(dmp) and W122-indole on different protein molecules are located at the interface at much shorter intermolecular distances (Re-W122(indole) = 6.9 Å, dmp-W122(indole) = 3.5 Å, and Re- Cu = 14.0 Å) than within single protein folds. Whereas forward ET is accelerated by hopping through W122, BET is retarded by a space jump at the interface that lacks specific interactions or water molecules. These findings on interfacial electron hopping in (Re126W122CuI)2 shed new light on optimal redox-unit placements required for functional long-range charge separation in protein complexes. (en)
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| Title
| - Tryptophan-Accelerated Electron Flow Across a ProteinProtein Interface
- Tryptophan-Accelerated Electron Flow Across a ProteinProtein Interface (en)
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| skos:prefLabel
| - Tryptophan-Accelerated Electron Flow Across a ProteinProtein Interface
- Tryptophan-Accelerated Electron Flow Across a ProteinProtein Interface (en)
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| skos:notation
| - RIV/61388955:_____/13:00397877!RIV14-MSM-61388955
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| http://linked.open...avai/predkladatel
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| http://linked.open...avai/riv/aktivita
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| http://linked.open...avai/riv/aktivity
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| http://linked.open...iv/cisloPeriodika
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| http://linked.open...vai/riv/dodaniDat
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| http://linked.open...aciTvurceVysledku
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| http://linked.open.../riv/druhVysledku
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| http://linked.open...iv/duvernostUdaju
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| http://linked.open...titaPredkladatele
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| http://linked.open...dnocenehoVysledku
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| http://linked.open...ai/riv/idVysledku
| - RIV/61388955:_____/13:00397877
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| http://linked.open...riv/jazykVysledku
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| http://linked.open.../riv/klicovaSlova
| - PSEUDOMONAS-AERUGINOSA AZURINS; CYTOCHROME B(5) INTERFACE; LASER MASS-SPECTROMETRY (en)
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| http://linked.open.../riv/klicoveSlovo
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| http://linked.open...odStatuVydavatele
| - US - Spojené státy americké
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| http://linked.open...ontrolniKodProRIV
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| http://linked.open...i/riv/nazevZdroje
| - Journal of the American Chemical Society
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| http://linked.open...in/vavai/riv/obor
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| http://linked.open...ichTvurcuVysledku
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| http://linked.open...cetTvurcuVysledku
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| http://linked.open...vavai/riv/projekt
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| http://linked.open...UplatneniVysledku
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| http://linked.open...v/svazekPeriodika
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| http://linked.open...iv/tvurceVysledku
| - Gray, H. B.
- Sokolová, L.
- Vlček jr., Antonín
- Williamson, H.
- Blanco-Rodríguez, A. M.
- Clark, I. P.
- Towrie, M.
- Winkler, J. R.
- Kaiser, J. T.
- Nikolovski, P.
- Takematsu, K.
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| http://linked.open...ain/vavai/riv/wos
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| issn
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| number of pages
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| http://bibframe.org/vocab/doi
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