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Application of NMR‐Spectroscopy to Retinal Proteins
Author(s) -
Engelhard Martin,
Bechinger Burkhard
Publication year - 1995
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.199500031
Subject(s) - chemistry , rhodopsin , bacteriorhodopsin , nuclear magnetic resonance spectroscopy , protonation , spectroscopy , isomerization , solid state nuclear magnetic resonance , nuclear magnetic resonance spectroscopy of nucleic acids , photoprotein , chemical shift , resonance raman spectroscopy , photochemistry , crystallography , retinal , stereochemistry , raman spectroscopy , fluorine 19 nmr , organic chemistry , transverse relaxation optimized spectroscopy , nuclear magnetic resonance , membrane , biochemistry , ion , physics , quantum mechanics , optics , calcium , catalysis
The application of NMR spectroscopy to the retinal proteins bacteriorhodopsin (BR) and rhodopsin is reviewed. 2 H‐, 15 N‐, and 13 C‐solid‐state NMR spectroscopy have contributed considerably to understanding the conformation and chemical environment of the protonated retinylidene Schiff base in BR as well as in rhodospin. The data from both pigments clarified the mechanism of the opsin shift which is quite different for rhodopsin and BR. An analysis of the chemical shifts of isotopically labeled aspartic acid, tyrosine, and proline incorporated into BR‐provided evidence for the protonation state of Asp and Tyr, and the isomerization state of the Xaa—Pro peptide bond, respectively. Solid‐state NMR spectroscopy was also applied to the investigation of the photocycle intermediates of BR, as well as bathorhodopsin and metarhodopsin II, which are formed after light‐activation of rhodopsin. Solution NMR spectroscopy of BR solubilized in detergents or organic solvents, as well as of opsin‐derived peptide segments, was also applied to the investigation of the two‐ and three‐dimensional structure of BR.