Double-quantum 13C nuclear magnetic resonance of bathorhodopsin, the first photointermediate in mammalian vision.
The 13C chemical shifts of the primary visual photointermediate bathorhodopsin have been observed by performing double-quantum magic-angle-spinning NMR at low temperature in the presence of illumination. Strong isomerization shifts have been observed upon the conversion of rhodopsin into bathorhodopsin.
Concistrè
Maria
M
School of Chemistry, University of Southampton, SO17 1BJ Southampton, UK.
Gansmüller
Axel
A
McLean
Neville
N
Johannessen
Ole G
OG
Marín Montesinos
Ildefonso
I
Bovee-Geurts
Petra H M
PH
Verdegem
Peter
P
Lugtenburg
Johan
J
Brown
Richard C D
RC
DeGrip
Willem J
WJ
Levitt
Malcolm H
MH
D000818:Animals; D002247:Carbon Isotopes / Q000737:chemistry; D003080:Cold Temperature; D007536:Isomerism; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D012243:Rhodopsin / Q000737:chemistry*; D014785:Vision, Ocular
D002247:Carbon Isotopes; C015017:bathorhodopsin; D012243:Rhodopsin