Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 118, Issue 17, Pages 4527-4534Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jp500919a
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Funding
- U.S. National Science Foundation [CHE-1213047, CHE-1264018]
- U.S. National Institutes of Health [R21EB009976-01]
- Biocentrum Helsinki
- Sigrid Juselius Foundation
- Academy of Finland
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1213047] Funding Source: National Science Foundation
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Red fluorescent proteins (RFPs) are indispensable tools for deep-tissue imaging, fluorescence resonance energy transfer applications, and super-resolution microscopy. Using time-resolved optical spectroscopy this study investigated photoinduced dynamics of three RFPs, KillerRed, mRFP, and DsRed. In all three RFPs, a new transient absorption intermediate was observed, which decays on a microsecond millisecond time scale. This intermediate is characterized by red-shifted absorption at 1.68-1.72 eV (lambda(max) = 720-740 nm). On the basis of electronic structure calculations, experimental evidence, and published literature, the chemical nature of the intermediate is assigned to an unusual open-shell dianionic chromophore (dianion-radical) formed via photoreduction. A doubly charged state that is not stable in the isolated (gas phase) chromophore is stabilized by the electrostatic field of the protein. Mechanistic implications for photobleaching, blinking, and phototoxicity are discussed.
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