@article {1010,
	title = {Light driven ultrafast electron transfer in oxidative redding of Green Fluorescent Proteins. [Protein Technology Facility]},
	journal = {Sci Rep},
	volume = {3},
	year = {2013},
	month = {2013},
	pages = {1580},
	abstract = {<p>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.</p>
},
	keywords = {Benzoquinones, Electron Transport, Green Fluorescent Proteins, Light, Oxidation-Reduction},
	issn = {2045-2322},
	doi = {10.1038/srep01580},
	author = {Saha, Ranajay and Verma, Pramod Kumar and Rakshit, Surajit and Saha, Suvrajit and Mayor, Satyajit and Pal, Samir Kumar}
}
@article {715,
	title = {Dynamic imaging of homo-FRET in live cells by fluorescence anisotropy microscopy.},
	journal = {Methods Enzymol},
	volume = {505},
	year = {2012},
	month = {2012},
	pages = {291-327},
	abstract = {<p>Multiple lipid and protein components of the plasma membrane of a living cell are organized, both compositionally and functionally, at different spatial and temporal scales. For instance, Rab protein domains in membranes the clathrin-coated pit, or the immunological synapse are exquisite examples of functional compartmentalization in cell membranes. These assemblies consist in part of nanoscale complexes of lipids and proteins and are necessary to facilitate some specific sorting and signaling functions. It is evident that cellular functions require a regulated spatiotemporal organization of components at the nanoscale, often comprising of countable number of molecular species. Here, we describe multiple homo-FRET-based imaging methods that provide information about nanoscale interactions between fluorescently tagged molecules in live cells, at optically resolved spatial resolution.</p>
},
	keywords = {Animals, Cell Membrane, Cell Tracking, Drosophila, Fluorescence Polarization, Fluorescence Resonance Energy Transfer, Green Fluorescent Proteins, Image Processing, Computer-Assisted, Lipid Metabolism, Microscopy, Confocal, Microscopy, Fluorescence},
	issn = {1557-7988},
	doi = {10.1016/B978-0-12-388448-0.00024-3},
	author = {Ghosh, Subhasri and Saha, Suvrajit and Goswami, Debanjan and Bilgrami, Sameera and Mayor, Satyajit}
}
