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Tryptophan-accelera...
Tryptophan-accelerated electron flow through proteins
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- Shih, Crystal (author)
- Beckman Institute, California Institute of Technology, Pasadena, USA
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- Museth, Anna Katrine (author)
- Beckman Institute, California Institute of Technology, Pasadena, USA
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- 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
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- Di Bilio, Angel J. (author)
- Beckman Institute, California Institute of Technology, Pasadena, USA
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- Sudhamsu, Jawahar (author)
- Department of Chemistry and Chemical Biology, Cornell University, Ithaca, USA
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- Crane, Brian R. (author)
- Department of Chemistry and Chemical Biology, Cornell University, Ithaca, USA
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- Ronayne, Kate L. (author)
- Central Laser Facility, STFC Rutherford Appleton Laboratory, Chilton, Didcot, Oxfordshire, UK
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- Towrie, Mike (author)
- Central Laser Facility, STFC Rutherford Appleton Laboratory, Chilton, Didcot, Oxfordshire, UK
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- Vlček Jr., Antonin (author)
- School of Biological and Chemical Sciences, Queen Mary, University of London, London, UK
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- Richards, John H. (author)
- Beckman Institute, California Institute of Technology, Pasadena, USA
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- Winkler, Jay R. (author)
- Beckman Institute, California Institute of Technology, Pasadena, USA
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- 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.
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In: Science. - : American Association for the Advancement of Science (AAAS). - 0036-8075 .- 1095-9203. ; 320:5884, s. 1760-1762
- Related links:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
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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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Shih, Crystal
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Museth, Anna Kat ...
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Abrahamsson, Mal ...
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Blanco-Rodriguez ...
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Di Bilio, Angel ...
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Sudhamsu, Jawaha ...
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show more...
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Crane, Brian R.
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Ronayne, Kate L.
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Towrie, Mike
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Vlček Jr., Anton ...
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Richards, John H ...
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Winkler, Jay R.
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Gray, Harry B.
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Linköping University