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In situ EPR spectroscopy of a bacterial membrane transporter using an expanded genetic code.

Department of Chemistry and Konstanz Research School Chemical Biology (KoRS-CB), University of Konstanz, Universitätsstraße 10, 78457 Konstanz, Germany. malte.drescher@uni-konstanz.de. Institute of Biophysics, Department of Physics & The Center for Biomolecular Magnetic Resonance (BMRZ), Goethe University Frankfurt, Max-von-Laue-Str. 1, 60438 Frankfurt/Main, Germany. joseph@biophysik.uni-frankfurt.de.

Chemical communications (Cambridge, England). 2021;(96):12980-12983
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Abstract

The membrane transporter BtuB is site-directedly spin labelled on the surface of living Escherichia coli via Diels-Alder click chemistry of the genetically encoded amino acid SCO-L-lysine. The previously introduced photoactivatable nitroxide PaNDA prevents off-target labelling, is used for distance measurements, and the temporally shifted activation of the nitroxide allows for advanced experimental setups. This study describes significant evolution of Diels-Alder-mediated spin labelling on cellular surfaces and opens up new vistas for the the study of membrane proteins.