ArticleJournal of the American Chemical Society2013
Tryptophan-accelerated electron flow across a protein-protein interface.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 52 citations in OpenAlex.
- CryoEM Structures of Native Quinol-Dependent Nitric Oxide Reductase in Resting and Quinol-Bound States.ACS bio & med chem Au · 2026Article
- The pH-dependence of copper(ii/i) reduction potentials in variants ofRSC advances · 2026Article
- Electron Transport through a Tryptophan Quadruplex in a Dimeric Azurin Construct.The journal of physical chemistry. B · 2026Article
- Molecular Design Principles for Achieving High-Efficiency Light-Induced Charge Separation at the Nanometer Scale.JACS Au · 2025Article
- Inter-cofactor protein remodeling rewires short-circuited transmembrane electron transfer.Communications chemistry · 2025Article
- Powering the Future: Unveiling the Secrets of Semiconductor Biointerfaces in Biohybrids for Semiartificial Photosynthesis.Artificial photosynthesis (Washington, D.C.) · 2025Review
- Time-series analysis of rhenium(I) organometallic covalent binding to a model protein for drug development.IUCrJ · 2024Article
- Tryptophan to Tryptophan Hole Hopping in an Azurin Construct.The journal of physical chemistry. B · 2024Article
- Review
- Photoinduced hole hopping through tryptophans in proteins.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Hole Hopping Across a Protein-Protein Interface.The journal of physical chemistry. B · 2019Article
- Two Tryptophans Are Better Than One in Accelerating Electron Flow through a Protein.ACS central science · 2019Article
- Characterization of the one-electron oxidized Cu(II)-salen complexes with a side chain aromatic ring: the effect of the indole ring on the Cu(II)-phenoxyl radical species.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Article
- Tuning electronic transport via hepta-alanine peptides junction by tryptophan doping.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Constraints on the Radical Cation Center of Cytochrome c Peroxidase for Electron Transfer from Cytochrome c.Biochemistry · 2016Article
- Electron flow through biological molecules: does hole hopping protect proteins from oxidative damage?Quarterly reviews of biophysics · 2015Review
- Photogeneration and Quenching of Tryptophan Radical in Azurin.The journal of physical chemistry. B · 2015Article
- Could tyrosine and tryptophan serve multiple roles in biological redox processes?Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2015Article
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Authors and funding
11 authors at 6 institutions in 4 countries.
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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 (<50 ns), followed by slow back ET to regenerate Cu(I) and ground-state Re(I) 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, (Re126W122Cu(I))2 and that the forward ET is accelerated by intermolecular electron hopping through the interfacial tryptophan: *Re//←W122←Cu(I), where // denotes a protein-protein interface. Solution mass spectrometry confirms a broad oligomer distribution with prevalent monomers and dimers, and the crystal structure of the Cu(II) form shows two Re126W122Cu(II) 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 (Re126W122Cu(I))2 shed new light on optimal redox-unit placements required for functional long-range charge separation in protein complexes.
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