Characterisation of Schiff base and chromophore in green proteorhodopsin by solid-state NMR.
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.
Pfleger
Nicole
N
Institute for Biophysical Chemistry, Centre for Biomolecular Magnetic Resonance, J. W. Goethe University, Max von Laue Str. 9, 60438, Frankfurt am Main, Germany.
Lorch
Mark
M
Woerner
Andreas C
AC
Shastri
Sarika
S
Glaubitz
Clemens
C
D007536:Isomerism; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008958:Models, Molecular; D012168:Retinal Pigments / Q000737:chemistry; D012243:Rhodopsin / Q000737:chemistry*; D025604:Rhodopsins, Microbial; D012545:Schiff Bases / Q000737:chemistry
D012168:Retinal Pigments; D025604:Rhodopsins, Microbial; D012545:Schiff Bases; C413548:proteorhodopsin; D012243:Rhodopsin