Literature DB >> 35857230

FTIR and Raman Spectroscopy of Rhodopsins.

Hideki Kandori1, Yasuhisa Mizutani2.   

Abstract

Vibrational spectroscopy such as FTIR and Raman spectroscopy is a powerful, sensitive, and informative method for studying protein structural changes in rhodopsins during their functions. The usefulness has been historically proven for the study of bacteriorhodopsin and bovine rhodopsin before their structural determination of rhodopsins. We now have atomic structures of many animal and microbial rhodopsins, and it is now important to know the structural dynamics of rhodopsins for function. FTIR and Raman spectroscopy provides useful information for this aim. In this chapter, we introduce the methods of FTIR and resonance Raman spectroscopy applied to rhodopsins. These vibrational methods offer deeper understanding on the mechanism how rhodopsins change their structures for function.
© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Hydrogen bond; Molecular vibration; Photointermediate; Structural dynamics

Mesh：

Substances：

Year:  2022        PMID： 35857230     DOI： 10.1007/978-1-0716-2329-9_10

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN： 1064-3745


  15 in total

Review 1.  Molecular reaction mechanisms of proteins monitored by time-resolved FTIR-spectroscopy.

Authors:  K Gerwert
Journal:  Biol Chem       Date:  1999 Jul-Aug       Impact factor: 3.915

Review 2.  Role of internal water molecules in bacteriorhodopsin.

Authors:  H Kandori
Journal:  Biochim Biophys Acta       Date:  2000-08-30

3.  Active internal waters in the bacteriorhodopsin photocycle. A comparative study of the L and M intermediates at room and cryogenic temperatures by infrared spectroscopy.

Authors:  Víctor A Lórenz-Fonfría; Yuji Furutani; Hideki Kandori
Journal:  Biochemistry       Date:  2008-03-06       Impact factor: 3.162

Review 4.  Microbial and animal rhodopsins: structures, functions, and molecular mechanisms.

Authors:  Oliver P Ernst; David T Lodowski; Marcus Elstner; Peter Hegemann; Leonid S Brown; Hideki Kandori
Journal:  Chem Rev       Date:  2013-12-23       Impact factor: 60.622

5.  Resonance Raman and infrared difference spectroscopy of retinal proteins.

Authors:  F Siebert
Journal:  Methods Enzymol       Date:  1990       Impact factor: 1.600

Review 6.  The Grateful Infrared: Sequential Protein Structural Changes Resolved by Infrared Difference Spectroscopy.

Authors:  Tilman Kottke; Víctor A Lórenz-Fonfría; Joachim Heberle
Journal:  J Phys Chem B       Date:  2016-12-01       Impact factor: 2.991

7.  Biomolecular vibrational spectroscopy.

Authors:  R A Mathies
Journal:  Methods Enzymol       Date:  1995       Impact factor: 1.600

Review 8.  Microbial Rhodopsins: Diversity, Mechanisms, and Optogenetic Applications.

Authors:  Elena G Govorunova; Oleg A Sineshchekov; Hai Li; John L Spudich
Journal:  Annu Rev Biochem       Date:  2017-03-09       Impact factor: 23.643

9.  Water molecules in the schiff base region of bacteriorhodopsin.

Authors:  Mikihiro Shibata; Taro Tanimoto; Hideki Kandori
Journal:  J Am Chem Soc       Date:  2003-11-05       Impact factor: 15.419

Review 10.  The form and function of channelrhodopsin.

Authors:  Karl Deisseroth; Peter Hegemann
Journal:  Science       Date:  2017-09-15       Impact factor: 47.728
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