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Characterisation of Schiff base and chromophore in green proteorhodopsin by solid-state NMR
Authors:Nicole Pfleger  Mark Lorch  Andreas C. Woerner  Sarika Shastri  Clemens Glaubitz
Affiliation:(1) Institute for Biophysical Chemistry, Centre for Biomolecular Magnetic Resonance, J. W. Goethe University, Max von Laue Str. 9, 60438 Frankfurt am Main, Germany;(2) Present address: Department of Chemistry, University of Hull, Hull, UK
Abstract:The proteorhodopsin family consists of hundreds of homologous retinal containing membrane proteins found in bacteria in the photic zone of the oceans. They are colour tuned to their environment and act as light-driven proton pumps with a potential energetic and regulatory function. Precise structural details are still unknown. Here, the green proteorhodopsin variant has been selected for a chemical shift analysis of retinal and Schiff base by solid-state NMR. Our data show that the chromophore exists in mainly all-trans configuration in the proteorhodopsin ground state. The optical absorption maximum together with retinal and Schiff base chemical shifts indicate a strong interaction network between chromophore and opsin. Electronic supplementary material The online version of this article (doi:) contains supplementary material, which is available to authorized users. Mark Lorch and Andreas C. Woerner contributed equally to this work.
Keywords:Proteorhodopsin  Solid-state NMR  Schiff base  Retinal
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