Light penetration and photoisomerization in rhodopsin studied by numerical simulations and double-quantum solid-state NMR spectroscopy.
The penetration of light into optically thick samples containing the G-protein-coupled receptor rhodopsin is studied by numerical finite-element simulations and double-quantum solid-state NMR experiments. Illumination with white light leads to the generation of the active bathorhodopsin photostate in the outer layer of the sample but generates a large amount of the side product, isorhodopsin, in the sample interior. The overall yield of bathorhodopsin is improved by using monochromatic 420 nm illumination and by mixing the sample with transparent glass beads. The implications of these findings on the interpretation of previously published rhodopsin NMR data are discussed.
Concistrè
Maria
M
School of Chemistry, University of Southampton, UK.
Gansmüller
Axel
A
McLean
Neville
N
Johannessen
Ole G
OG
Marín Montesinos
Ildefonso
I
Bovee-Geurts
Petra H M
PH
Brown
Richard C D
RC
DeGrip
Willem J
WJ
Levitt
Malcolm H
MH
D003198:Computer Simulation; D008027:Light; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D015394:Molecular Structure; D055668:Photochemical Processes / Q000528:radiation effects*; D011789:Quantum Theory; D012243:Rhodopsin / Q000737:chemistry* / Q000528:radiation effects*; D013237:Stereoisomerism
D012243:Rhodopsin