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Tryptophan-Accelerated Electron Flow Through Proteins
Abstract
Energy flow in biological structures often requires submillisecond charge transport over long molecular distances. Kinetics modeling suggests that charge-transfer rates can be greatly enhanced by multistep electron tunneling in which redox-active amino acid side chains act as intermediate donors or acceptors. We report transient optical and infrared spectroscopic experiments that quantify the extent to which an intervening tryptophan residue can facilitate electron transfer between distant metal redox centers in a mutant Pseudomonas aeruginosa azurin. Cu I oxidation by a photoexcited Re I -diimine at position 124 on a histidine(124)-glycine(123)-tryptophan(122)-methionine(121) β strand occurs in a few nanoseconds, fully two orders of magnitude faster than documented for single-step electron tunneling at a 19 angstrom donor-acceptor distance.
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Stubbe, J., Nocera, D. G., Yee, C. S., & Chang, M. C. Y. (2003) · Chemical Reviews · doi:10.1021/cr020421u · Cited by 823
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Delor, M., Scattergood, P. A., Sazanovich, I. V., Parker, A. W., Greetham, G. M., Meijer, A. J. H. M., Towrie, M., & Weinstein, J. A. (2014) · Science · doi:10.1126/science.1259995 · Cited by 199
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Metadata
- Authors
- Shih, C., Museth, A. K., Abrahamsson, M., Blanco-Rodriguez, A. M., Di Bilio, A. J., Sudhamsu, J., Crane, B. R., Ronayne, K. L., Towrie, M., Vlček, A., Richards, J. H., Winkler, J. R., & Gray, H. B.
- Venue
- Science
- Published
- 2008-06-27
- Volume
- 320
- Issue
- 5884
- Pages
- 1760-1762
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2071595256
- Cited by
- 409
- References
- 1
- FWCI
- 22.34
- Type
- journal article
- Language
- en
- Open access
- closed
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- Shih, C., Museth, A. K., Abrahamsson, M., Blanco-Rodriguez, A. M., Di Bilio, A. J., Sudhamsu, J., Crane, B. R., Ronayne, K. L., Towrie, M., Vlček, A., Richards, J. H., Winkler, J. R., & Gray, H. B. (2008). Tryptophan-Accelerated Electron Flow Through Proteins. Science. https://doi.org/10.1126/science.1158241
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.