Oriented Insertion of ESR-Containing Hybrid Proteins in Proteoliposomes

Autor: Lada E. Petrovskaya, Evgeniy P. Lukashev, Mahir D. Mamedov, Elena A. Kryukova, Sergei P. Balashov, Dmitry A. Dolgikh, Andrei B. Rubin, Mikhail P. Kirpichnikov, Sergey A. Siletsky

Publikováno v: International Journal of Molecular Sciences; Volume 24; Issue 8; Pages: 7369

Microbial rhodopsins comprise a diverse family of retinal-containing membrane proteins that convert absorbed light energy to transmembrane ion transport or sensory signals. Incorporation of these proteins in proteoliposomes allows their properties to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::301e47eead7242525e78736f9362d2d4

Application of direct electrometry in studies of microbial rhodopsins reconstituted in proteoliposomes

Autor: Sergey A. Siletsky, Mahir D. Mamedov, Evgeniy P. Lukashev, Sergei P. Balashov, Lada E. Petrovskaya

Publikováno v: Biophysical reviews. 14(4)

Microbial rhodopsins are the family of retinal-containing proteins that perform primarily the light-driven transmembrane ion transport and sensory functions. They are widely distributed in nature and can be used for optogenetic control of the cellula

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aaadd60c55d4be7a9a578f7fdb0a9592
https://pubmed.ncbi.nlm.nih.gov/36124261

Proton transfer reactions in donor site mutants of ESR, a retinal protein from Exiguobacterium sibiricum

Autor: Lada E, Petrovskaya, Evgeniy P, Lukashev, Sergey A, Siletsky, Eleonora S, Imasheva, Jennifer M, Wang, Mahir D, Mamedov, Elena A, Kryukova, Dmitriy A, Dolgikh, Andrei B, Rubin, Mikhail P, Kirpichnikov, Sergei P, Balashov, Janos K, Lanyi

Publikováno v: Journal of Photochemistry and Photobiology B: Biology. 234:112529

Light-driven proton transport by microbial retinal proteins such as archaeal bacteriorhodopsin involves carboxylic residues as internal proton donors to the catalytic center which is a retinal Schiff base (SB). The proton donor, Asp96 in bacteriorhod

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c710818a78cbc8ccdfc982def69e4532
https://doi.org/10.1016/j.jphotobiol.2022.112529

Elimination of proton donor strongly affects directionality and efficiency of proton transport in ESR, a light-driven proton pump from Exiguobacterium sibiricum

Autor: Sergei P. Balashov, Andrei B. Rubin, D. A. Dolgikh, Mahir D. Mamedov, E. P. Lukashev, Mikhail P. Kirpichnikov, Sergey A. Siletsky, Lada E. Petrovskaya

Publikováno v: Biochimica et biophysica acta. Bioenergetics. 1860(1)

ESR from Exiguobacterium sibiricum is a retinal protein which functions as a proton pump. Unusual feature of ESR is that a lysine residue is present at a site for the internal proton donor, which in other proton pumps is a carboxylic residue. Replace

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d3316baeb7e34ba5b971eeff29cc388
https://pubmed.ncbi.nlm.nih.gov/30497582

Directed evolution of a far-red fluorescent rhodopsin

Autor: Eleonora S. Imasheva, Timothy M. Wannier, Frances H. Arnold, Adam Z. Rosenthal, Janos K. Lanyi, R. Scott McIsaac, Sergei P. Balashov, Martin K. M. Engqvist, Nicholas C. Flytzanis, Viviana Gradinaru, Lukas Herwig

Publikováno v: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
McIsaac, RS; Engqvist, MKM; Wannier, T; Rosenthal, AZ; Herwig, L; Flytzanis, NC; et al.(2014). Directed evolution of a far-red fluorescent rhodopsin. Proceedings of the National Academy of Sciences of the United States of America, 111(36), 13034-13039. doi: 10.1073/pnas.1413987111. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/2ct5x0p3

Microbial rhodopsins are a diverse group of photoactive transmembrane proteins found in all three domains of life. A member of this protein family, Archaerhodopsin-3 (Arch) of halobacterium Halorubrum sodomense, was recently shown to function as a fl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54d2dc59a320d9a6845557d3c8d87349