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Light driven ultrafast electron transfer in oxidative redding of Green Fluorescent Proteins.
Sci Rep 2013; 3:1580SR

Abstract

Fluorescent proteins undergoing green to red (G/R) photoconversion have proved to be potential tools for investigating dynamic processes in living cells and for photo-localization nanoscopy. However, the photochemical reaction during light induced G/R photoconversion of fluorescent proteins remains unclear. Here we report the direct observation of ultrafast time-resolved electron transfer (ET) during the photoexcitation of the fluorescent proteins EGFP and mEos2 in presence of electron acceptor, p-benzoquinone (BQ). Our results show that in the excited state, the neutral EGFP chromophore accepts electrons from an anionic electron donor, Glu222, and G/R photoconversion is facilitated by ET to nearby electron acceptors. By contrast, mEos2 fails to produce the red emitting state in the presence of BQ; ET depletes the excited state configuration en route to the red-emitting fluorophore. These results show that ultrafast ET plays a pivotal role in multiple photoconversion mechanisms and provide a method to modulate the G/R photoconversion process.

Authors+Show Affiliations

Unit for Nano Science & Technology, Department of Chemical, Biological & Macromolecular Sciences, S. N. Bose National Centre for Basic Sciences, Block JD, Sector III, Salt Lake, Kolkata, India.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

23552964

Citation

Saha, Ranajay, et al. "Light Driven Ultrafast Electron Transfer in Oxidative Redding of Green Fluorescent Proteins." Scientific Reports, vol. 3, 2013, p. 1580.
Saha R, Verma PK, Rakshit S, et al. Light driven ultrafast electron transfer in oxidative redding of Green Fluorescent Proteins. Sci Rep. 2013;3:1580.
Saha, R., Verma, P. K., Rakshit, S., Saha, S., Mayor, S., & Pal, S. K. (2013). Light driven ultrafast electron transfer in oxidative redding of Green Fluorescent Proteins. Scientific Reports, 3, p. 1580. doi:10.1038/srep01580.
Saha R, et al. Light Driven Ultrafast Electron Transfer in Oxidative Redding of Green Fluorescent Proteins. Sci Rep. 2013;3:1580. PubMed PMID: 23552964.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Light driven ultrafast electron transfer in oxidative redding of Green Fluorescent Proteins. AU - Saha,Ranajay, AU - Verma,Pramod Kumar, AU - Rakshit,Surajit, AU - Saha,Suvrajit, AU - Mayor,Satyajit, AU - Pal,Samir Kumar, PY - 2012/12/18/received PY - 2013/03/07/accepted PY - 2013/4/5/entrez PY - 2013/4/5/pubmed PY - 2013/10/18/medline SP - 1580 EP - 1580 JF - Scientific reports JO - Sci Rep VL - 3 N2 - Fluorescent proteins undergoing green to red (G/R) photoconversion have proved to be potential tools for investigating dynamic processes in living cells and for photo-localization nanoscopy. However, the photochemical reaction during light induced G/R photoconversion of fluorescent proteins remains unclear. Here we report the direct observation of ultrafast time-resolved electron transfer (ET) during the photoexcitation of the fluorescent proteins EGFP and mEos2 in presence of electron acceptor, p-benzoquinone (BQ). Our results show that in the excited state, the neutral EGFP chromophore accepts electrons from an anionic electron donor, Glu222, and G/R photoconversion is facilitated by ET to nearby electron acceptors. By contrast, mEos2 fails to produce the red emitting state in the presence of BQ; ET depletes the excited state configuration en route to the red-emitting fluorophore. These results show that ultrafast ET plays a pivotal role in multiple photoconversion mechanisms and provide a method to modulate the G/R photoconversion process. SN - 2045-2322 UR - https://www.unboundmedicine.com/medline/citation/23552964/Light_driven_ultrafast_electron_transfer_in_oxidative_redding_of_Green_Fluorescent_Proteins_ L2 - http://dx.doi.org/10.1038/srep01580 DB - PRIME DP - Unbound Medicine ER -