Literature DB >> 35857221

Microbial Rhodopsins.

Valentin Gordeliy1, Kirill Kovalev2,3,4,5,6, Ernst Bamberg7, Francisco Rodriguez-Valera5,8, Egor Zinovev5, Dmitrii Zabelskii5, Alexey Alekseev5, Riccardo Rosselli9, Ivan Gushchin5, Ivan Okhrimenko5.   

Abstract

The first microbial rhodopsin, a light-driven proton pump bacteriorhodopsin from Halobacterium salinarum (HsBR), was discovered in 1971. Since then, this seven-α-helical protein, comprising a retinal molecule as a cofactor, became a major driver of groundbreaking developments in membrane protein research. However, until 1999 only a few archaeal rhodopsins, acting as light-driven proton and chloride pumps and also photosensors, were known. A new microbial rhodopsin era started in 2000 when the first bacterial rhodopsin, a proton pump, was discovered. Later it became clear that there are unexpectedly many rhodopsins, and they are present in all the domains of life and even in viruses. It turned out that they execute such a diversity of functions while being "nearly the same." The incredible evolution of the research area of rhodopsins and the scientific and technological potential of the proteins is described in the review with a focus on their function-structure relationships.
© 2022. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Entities:  

Keywords:  Ion transport; Membrane protein; Optogenetics; Retinal; Rhodopsin

Mesh:

Substances:

Year:  2022        PMID: 35857221     DOI: 10.1007/978-1-0716-2329-9_1

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


  180 in total

1.  Structural changes in bacteriorhodopsin during ion transport at 2 angstrom resolution.

Authors:  H Luecke; B Schobert; H T Richter; J P Cartailler; J K Lanyi
Journal:  Science       Date:  1999-10-08       Impact factor: 47.728

2.  Helix deformation is coupled to vectorial proton transport in the photocycle of bacteriorhodopsin.

Authors:  A Royant; K Edman; T Ursby; E Pebay-Peyroula; E M Landau; R Neutze
Journal:  Nature       Date:  2000-08-10       Impact factor: 49.962

3.  Two photosystems controlling behavioural responses of Halobacterium halobium.

Authors:  E Hildebrand; N Dencher
Journal:  Nature       Date:  1975-09-04       Impact factor: 49.962

4.  Three-dimensional model of purple membrane obtained by electron microscopy.

Authors:  R Henderson; P N Unwin
Journal:  Nature       Date:  1975-09-04       Impact factor: 49.962

5.  Two possible roles of bacteriorhodopsin; a comparative study of strains of Halobacterium halobium differing in pigmentation.

Authors:  A Matsuno-Yagi; Y Mukohata
Journal:  Biochem Biophys Res Commun       Date:  1977-09-09       Impact factor: 3.575

6.  Lipidic cubic phases: a novel concept for the crystallization of membrane proteins.

Authors:  E M Landau; J P Rosenbusch
Journal:  Proc Natl Acad Sci U S A       Date:  1996-12-10       Impact factor: 11.205

7.  X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases.

Authors:  E Pebay-Peyroula; G Rummel; J P Rosenbusch; E M Landau
Journal:  Science       Date:  1997-09-12       Impact factor: 47.728

8.  Rhodopsin-like protein from the purple membrane of Halobacterium halobium.

Authors:  D Oesterhelt; W Stoeckenius
Journal:  Nat New Biol       Date:  1971-09-29

9.  Crystallographic structure of the K intermediate of bacteriorhodopsin: conservation of free energy after photoisomerization of the retinal.

Authors:  Brigitte Schobert; Jill Cupp-Vickery; Viktor Hornak; Steven Smith; Janos Lanyi
Journal:  J Mol Biol       Date:  2002-08-23       Impact factor: 5.469

10.  Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution.

Authors:  H Luecke; H T Richter; J K Lanyi
Journal:  Science       Date:  1998-06-19       Impact factor: 47.728

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.