title: Turning On and Off Photoinduced Electron Transfer in Fluorescent Proteins by π-Stacking, Halide Binding, and Tyr145 Mutations.
abstract: Photoinduced 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.
authors.affiliation: Shemiakin-Ovchinnikov Institute of Bioorganic Chemistry , Moscow 117997, Russia.|Nizhny Novgorod State Medical Academy , Nizhny Novgorod 603005, Russia.
authors.forename: Alexey M
authors.initials: AM
authors.lastname: Bogdanov
authors.affiliation: Department of Chemistry, University of Southern California , Los Angeles, California 90089-0482, United States.
authors.forename: Atanu
authors.initials: A
authors.lastname: Acharya
authors.affiliation: Shemiakin-Ovchinnikov Institute of Bioorganic Chemistry , Moscow 117997, Russia.
authors.forename: Anastasia V
authors.initials: AV
authors.lastname: Titelmayer
authors.affiliation: Shemiakin-Ovchinnikov Institute of Bioorganic Chemistry , Moscow 117997, Russia.
authors.forename: Anastasia V
authors.initials: AV
authors.lastname: Mamontova
authors.affiliation: Department of Chemistry, Boston University , Boston, Massachusetts 02215, United States.
authors.forename: Ksenia B
authors.initials: KB
authors.lastname: Bravaya
authors.affiliation: Department of Chemistry, Rice University , Houston, Texas 77251-1892, United States.
authors.forename: Anatoly B
authors.initials: AB
authors.lastname: Kolomeisky
authors.affiliation: Shemiakin-Ovchinnikov Institute of Bioorganic Chemistry , Moscow 117997, Russia.|Nizhny Novgorod State Medical Academy , Nizhny Novgorod 603005, Russia.
authors.forename: Konstantin A
authors.initials: KA
authors.lastname: Lukyanov
authors.affiliation: Department of Chemistry, University of Southern California , Los Angeles, California 90089-0482, United States.
authors.forename: Anna I
authors.initials: AI
authors.lastname: Krylov
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics*; D001965:Bromides / Q000737:chemistry; D002712:Chlorides / Q000737:chemistry; D005459:Fluorides / Q000737:chemistry; D049452:Green Fluorescent Proteins / Q000737:chemistry* / Q000235:genetics*; D057809:HEK293 Cells; D006801:Humans; D007454:Iodides / Q000737:chemistry; D008164:Luminescent Proteins / Q000737:chemistry* / Q000235:genetics*; D008856:Microscopy, Fluorescence; D008958:Models, Molecular; D062105:Molecular Docking Simulation; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D010084:Oxidation-Reduction; D055668:Photochemical Processes; D011485:Protein Binding; D013816:Thermodynamics; D014443:Tyrosine / Q000737:chemistry / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D001965:Bromides; D002712:Chlorides; D007454:Iodides; D008164:Luminescent Proteins; C485184:enhanced green fluorescent protein; C054562:yellow fluorescent protein, Bacteria; D049452:Green Fluorescent Proteins; D014443:Tyrosine; D005459:Fluorides