Turning On and Off Photoinduced Electron Transfer in Fluorescent Proteins by π-Stacking, Halide Binding, and Tyr145 Mutations

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dc.citation.firstpage4807en_US
dc.citation.issueNumber14en_US
dc.citation.journalTitleJournal of the American Chemical Societyen_US
dc.citation.lastpage4817en_US
dc.citation.volumeNumber138en_US
dc.contributor.authorBogdanov, Alexey M.en_US
dc.contributor.authorAcharya, Atanuen_US
dc.contributor.authorTitelmayer, Anastasia V.en_US
dc.contributor.authorMamontova, Anastasia V.en_US
dc.contributor.authorBravaya, Ksenia B.en_US
dc.contributor.authorKolomeisky, Anatoly B.en_US
dc.contributor.authorLukyanov, Konstantin A.en_US
dc.contributor.authorKrylov, Anna I.en_US
dc.date.accessioned2016-06-22T16:28:31Zen_US
dc.date.available2016-06-22T16:28:31Zen_US
dc.date.issued2016en_US
dc.description.abstractPhotoinduced electron transfer in fluorescent proteins from the GFP family can be regarded either as an asset facilitating new applications or as a nuisance leading to the loss of optical output. Photooxidation commonly results in green-to-red photoconversion called oxidative redding. We discovered that yellow FPs do not undergo redding; however, the redding is restored upon halide binding. Calculations of the energetics of one-electron oxidation and possible electron transfer (ET) pathways suggested that excited-state ET proceeds through a hopping mechanism via Tyr145. In YFPs, the π-stacking of the chromophore with Tyr203 reduces its electron-donating ability, which can be restored by halide binding. Point mutations confirmed that Tyr145 is a key residue controlling ET. Substitution of Tyr145 by less-efficient electron acceptors resulted in highly photostable mutants. This strategy (i.e., calculation and disruption of ET pathways by mutations) may represent a new approach toward enhancing photostability of Fps.en_US
dc.identifier.citationBogdanov, Alexey M., Acharya, Atanu, Titelmayer, Anastasia V., et al.. "Turning On and Off Photoinduced Electron Transfer in Fluorescent Proteins by π-Stacking, Halide Binding, and Tyr145 Mutations." <i>Journal of the American Chemical Society,</i> 138, no. 14 (2016) American Chemical Society: 4807-4817. http://dx.doi.org/10.1021/jacs.6b00092.en_US
dc.identifier.doihttp://dx.doi.org/10.1021/jacs.6b00092en_US
dc.identifier.urihttps://hdl.handle.net/1911/90516en_US
dc.language.isoengen_US
dc.publisherAmerican Chemical Societyen_US
dc.rightsThis is an open access article published under an ACS AuthorChoice License, which permits copying and redistribution of the article or any adaptations for non-commercial purposes.en_US
dc.rights.urihttp://pubs.acs.org/page/policy/authorchoice_termsofuse.htmlen_US
dc.titleTurning On and Off Photoinduced Electron Transfer in Fluorescent Proteins by π-Stacking, Halide Binding, and Tyr145 Mutationsen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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