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Tryptophan-accelerated electron flow through proteins

Shih, Crystal (author)
Beckman Institute, California Institute of Technology, Pasadena, USA
Museth, Anna Katrine (author)
Beckman Institute, California Institute of Technology, Pasadena, USA
Abrahamsson, Malin (author)
Beckman Institute, California Institute of Technology, Pasadena, USA
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Blanco-Rodriguez, Ana Maria (author)
School of Biological and Chemical Sciences, Queen Mary, University of London, London, UK
Di Bilio, Angel J. (author)
Beckman Institute, California Institute of Technology, Pasadena, USA
Sudhamsu, Jawahar (author)
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, USA
Crane, Brian R. (author)
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, USA
Ronayne, Kate L. (author)
Central Laser Facility, STFC Rutherford Appleton Laboratory, Chilton, Didcot, Oxfordshire, UK
Towrie, Mike (author)
Central Laser Facility, STFC Rutherford Appleton Laboratory, Chilton, Didcot, Oxfordshire, UK
Vlček Jr., Antonin (author)
School of Biological and Chemical Sciences, Queen Mary, University of London, London, UK
Richards, John H. (author)
Beckman Institute, California Institute of Technology, Pasadena, USA
Winkler, Jay R. (author)
Beckman Institute, California Institute of Technology, Pasadena, USA
Gray, Harry B. (author)
Beckman Institute, California Institute of Technology, Pasadena, USA
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 (creator_code:org_t)
American Association for the Advancement of Science (AAAS), 2008
2008
English.
In: Science. - : American Association for the Advancement of Science (AAAS). - 0036-8075 .- 1095-9203. ; 320:5884, s. 1760-1762
Related links:
https://urn.kb.se/re...
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https://doi.org/10.1...
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  • Journal article (peer-reviewed)
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  • 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. CuI oxidation by a photoexcited ReI-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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