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Action spectroscopy of the isolated red Kaede fluorescent protein chromophore.
- Source :
-
The Journal of chemical physics [J Chem Phys] 2021 Sep 28; Vol. 155 (12), pp. 124304. - Publication Year :
- 2021
-
Abstract
- Incorporation of fluorescent proteins into biochemical systems has revolutionized the field of bioimaging. In a bottom-up approach, understanding the photophysics of fluorescent proteins requires detailed investigations of the light-absorbing chromophore, which can be achieved by studying the chromophore in isolation. This paper reports a photodissociation action spectroscopy study on the deprotonated anion of the red Kaede fluorescent protein chromophore, demonstrating that at least three isomers-assigned to deprotomers-are generated in the gas phase. Deprotomer-selected action spectra are recorded over the S <subscript>1</subscript> ← S <subscript>0</subscript> band using an instrument with differential mobility spectrometry coupled with photodissociation spectroscopy. The spectrum for the principal phenoxide deprotomer spans the 480-660 nm range with a maximum response at ≈610 nm. The imidazolate deprotomer has a blue-shifted action spectrum with a maximum response at ≈545 nm. The action spectra are consistent with excited state coupled-cluster calculations of excitation wavelengths for the deprotomers. A third gas-phase species with a distinct action spectrum is tentatively assigned to an imidazole tautomer of the principal phenoxide deprotomer. This study highlights the need for isomer-selective methods when studying the photophysics of biochromophores possessing several deprotonation sites.
Details
- Language :
- English
- ISSN :
- 1089-7690
- Volume :
- 155
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- The Journal of chemical physics
- Publication Type :
- Academic Journal
- Accession number :
- 34598549
- Full Text :
- https://doi.org/10.1063/5.0063258