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Literature DB >> 18642911

Double-quantum 13C nuclear magnetic resonance of bathorhodopsin, the first photointermediate in mammalian vision.

Maria Concistrè¹, Axel Gansmüller, Neville McLean, Ole G Johannessen, Ildefonso Marín Montesinos, Petra H M Bovee-Geurts, Peter Verdegem, Johan Lugtenburg, Richard C D Brown, Willem J DeGrip, Malcolm H Levitt.

Abstract

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.

Entities: Chemical Gene Species

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Year: 2008 PMID： 18642911 DOI： 10.1021/ja803801u

Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419

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Cited

5 in total

1. A large geometric distortion in the first photointermediate of rhodopsin, determined by double-quantum solid-state NMR.

Authors: Maria Concistrè; Ole G Johannessen; Neville McLean; Petra H M Bovee-Geurts; Richard C D Brown; Willem J Degrip; Malcolm H Levitt
Journal: J Biomol NMR Date: 2012-05-26 Impact factor: 2.835

2. QM/MM study of the structure, energy storage, and origin of the bathochromic shift in vertebrate and invertebrate bathorhodopsins.

Authors: Sivakumar Sekharan; Keiji Morokuma
Journal: J Am Chem Soc Date: 2011-03-10 Impact factor: 15.419

Double-quantum 13C nuclear magnetic resonance of bathorhodopsin, the first photointermediate in mammalian vision.

1. A large geometric distortion in the first photointermediate of rhodopsin, determined by double-quantum solid-state NMR.

2. QM/MM study of the structure, energy storage, and origin of the bathochromic shift in vertebrate and invertebrate bathorhodopsins.

Review 3. Structure and function of G protein-coupled receptors using NMR spectroscopy.

Review 4. Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.

Review 5. Synthesis and use of stable isotope enriched retinals in the field of vitamin A.