Ultrafast excited-state dynamics of the photoswitchable protein dronpa

Eduard Fron; Cristina Flors; Gerd Schweitzer; Satoshi Habuchi; Hideaki Mizuno; Ryoko Ando; Frans C. De Schryver; Atsushi Miyawaki; Johan Hofkens

doi:10.1021/ja069365v

Ultrafast excited-state dynamics of the photoswitchable protein dronpa

Eduard Fron, Cristina Flors^*, Gerd Schweitzer, Satoshi Habuchi, Hideaki Mizuno, Ryoko Ando, Frans C. De Schryver, Atsushi Miyawaki, Johan Hofkens

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

70 Scopus citations

Abstract

Dronpa is a photoswitchable protein from the family of green fluorescent proteins (GFPs). Photoswitching involves forward and backward proton transfer between a bright deprotonated form (B) and a dark protonated form (A₂). We have used femtosecond transient absorption spectroscopy to determine the kinetics of the first step of the photoconversion from the dark to the bright form, which we have measured as 4 ps. The 2-fold isotope effect on the kinetics of this process shows that excited-state proton transfer (ESPT) is involved in this step. It was also demonstrated that the acid-induced protonated form A₁ and the photoconverted protonated form A₂ are two distinct spectroscopic species.

Original language	English (US)
Pages (from-to)	4870-4871
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	129
Issue number	16
DOIs	https://doi.org/10.1021/ja069365v
State	Published - Apr 25 2007
Externally published	Yes

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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title = "Ultrafast excited-state dynamics of the photoswitchable protein dronpa",

abstract = "Dronpa is a photoswitchable protein from the family of green fluorescent proteins (GFPs). Photoswitching involves forward and backward proton transfer between a bright deprotonated form (B) and a dark protonated form (A2). We have used femtosecond transient absorption spectroscopy to determine the kinetics of the first step of the photoconversion from the dark to the bright form, which we have measured as 4 ps. The 2-fold isotope effect on the kinetics of this process shows that excited-state proton transfer (ESPT) is involved in this step. It was also demonstrated that the acid-induced protonated form A1 and the photoconverted protonated form A2 are two distinct spectroscopic species.",

author = "Eduard Fron and Cristina Flors and Gerd Schweitzer and Satoshi Habuchi and Hideaki Mizuno and Ryoko Ando and {De Schryver}, {Frans C.} and Atsushi Miyawaki and Johan Hofkens",

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T1 - Ultrafast excited-state dynamics of the photoswitchable protein dronpa

AU - Fron, Eduard

AU - Flors, Cristina

AU - Schweitzer, Gerd

AU - Habuchi, Satoshi

AU - Mizuno, Hideaki

AU - Ando, Ryoko

AU - De Schryver, Frans C.

AU - Miyawaki, Atsushi

AU - Hofkens, Johan

PY - 2007/4/25

Y1 - 2007/4/25

N2 - Dronpa is a photoswitchable protein from the family of green fluorescent proteins (GFPs). Photoswitching involves forward and backward proton transfer between a bright deprotonated form (B) and a dark protonated form (A2). We have used femtosecond transient absorption spectroscopy to determine the kinetics of the first step of the photoconversion from the dark to the bright form, which we have measured as 4 ps. The 2-fold isotope effect on the kinetics of this process shows that excited-state proton transfer (ESPT) is involved in this step. It was also demonstrated that the acid-induced protonated form A1 and the photoconverted protonated form A2 are two distinct spectroscopic species.

AB - Dronpa is a photoswitchable protein from the family of green fluorescent proteins (GFPs). Photoswitching involves forward and backward proton transfer between a bright deprotonated form (B) and a dark protonated form (A2). We have used femtosecond transient absorption spectroscopy to determine the kinetics of the first step of the photoconversion from the dark to the bright form, which we have measured as 4 ps. The 2-fold isotope effect on the kinetics of this process shows that excited-state proton transfer (ESPT) is involved in this step. It was also demonstrated that the acid-induced protonated form A1 and the photoconverted protonated form A2 are two distinct spectroscopic species.

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Ultrafast excited-state dynamics of the photoswitchable protein dronpa

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