Far-Red Emission of mPlum Fluorescent Protein Results from Excited-State Interconversion between Chromophore Hydrogen-Bonding States
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SCOPUS
- Title
- Far-Red Emission of mPlum Fluorescent Protein Results from Excited-State Interconversion between Chromophore Hydrogen-Bonding States
- Authors
- Yoon, E; Konold, PE; Lee, J; Joo, T; Jimenez, R
- Date Issued
- 2016-06-16
- Publisher
- American Chemical Society
- Abstract
- Fluorescent proteins with large Stokes shifted emission beyond 600 nm are actively sought for live-cell imaging applications. The mechanism of excited-state relaxation leading to the Stokes shift in the mPlum fluorescent protein, which emits at a peak wavelength of 650 nm, has been previously investigated by both ultrafast spectroscopy and theoretical methods. Here, we report that femtosecond time-resolved area-normalized emission spectra of mPlum show a clear isoemissive point. This feature can only result from a system with two emitting states, rather than a system that undergoes a continuous spectral red shift, for example, as expected from typical solvation. Global analysis of the femtosecond time-resolved fluorescence spectra reveals time constants associated with chromophore relaxation, excited-state population transfer, and an excited-state lifetime of the final state. The observations confirm the findings of recent quantum chemical calculations on mPlum.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/37588
- DOI
- 10.1021/ACS.JPCLETT.6B00823
- ISSN
- 1948-7185
- Article Type
- Article
- Citation
- The Journal of Physical Chemistry Letters, vol. 7, no. 12, page. 2170 - 2174, 2016-06-16
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