Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Eleonora S, Imasheva"'
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
https://doi.org/10.1016/j.jphotobiol.2022.112529
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
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
Autor:
D. A. Dolgikh, Jennifer M. Wang, Andrei B. Rubin, Eleonora S. Imasheva, Sergei P. Balashov, Lada E. Petrovskaya, E. P. Lukashev, Mikhail P. Kirpichnikov, Andrei K. Dioumaev, S. V. Sychev, Janos K. Lanyi
Publikováno v:
Journal of Biological Chemistry. 288:21254-21265
A lysine instead of the usual carboxyl group is in place of the internal proton donor to the retinal Schiff base in the light-driven proton pump of Exiguobacterium sibiricum (ESR). The involvement of this lysine in proton transfer is indicated by the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::188188c68008dbf581dbc557aa95ab08
https://doi.org/10.1074/jbc.m113.465138
https://doi.org/10.1074/jbc.m113.465138
Publikováno v:
The Journal of Membrane Biology
Imasheva, Eleonora S.; Balashov, Sergei P.; Wang, Jennifer M.; & Lanyi, Janos K.(2011). Removal and Reconstitution of the Carotenoid Antenna of Xanthorhodopsin. The Journal of Membrane Biology, 239(1), pp 95-104. doi: 10.1007/s00232-010-9322-x. Retrieved from: http://www.escholarship.org/uc/item/1gc1q608
Imasheva, Eleonora S.; Balashov, Sergei P.; Wang, Jennifer M.; & Lanyi, Janos K.(2011). Removal and Reconstitution of the Carotenoid Antenna of Xanthorhodopsin. The Journal of Membrane Biology, 239(1), pp 95-104. doi: 10.1007/s00232-010-9322-x. Retrieved from: http://www.escholarship.org/uc/item/1gc1q608
Salinixanthin, a C(40)-carotenoid acyl glycoside, serves as a light-harvesting antenna in the retinal-based proton pump xanthorhodopsin of Salinibacter ruber. In the crystallographic structure of this protein, the conjugated chain of salinixanthin is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3d90f7289e4414b8a75d379a8bfd2e06
https://doi.org/10.1007/s00232-010-9322-x
https://doi.org/10.1007/s00232-010-9322-x
Autor:
Kwang-Hwan Jung, Synnøve Liaaen-Jensen, Sergei P. Balashov, Ah Reum Choi, Eleonora S. Imasheva, Janos K. Lanyi
Publikováno v:
Biochemistry. 49:9792-9799
In previous work, we reconstituted salinixanthin, the C(40)-carotenoid acyl glycoside that serves as a light-harvesting antenna to the light-driven proton pump xanthorhodopsin, into a different protein, gloeobacter rhodopsin expressed in Escherichia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46f85608f9722d7ebbe2464c0e860a70
https://doi.org/10.1021/bi1014166
https://doi.org/10.1021/bi1014166
Publikováno v:
Biochemistry. 48:10948-10955
We show that salinixanthin, the light-harvesting carotenoid antenna of xanthorhodopsin, can be reconstituted into the retinal protein from Gloeobacter violaceus expressed in Escherichia coli. Reconstitution of gloeobacter rhodopsin with the carotenoi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4daba9ab4cbf4ecf693fc3c212a7d567
https://doi.org/10.1021/bi901552x
https://doi.org/10.1021/bi901552x
Autor:
Hartmut Luecke, Sergei P. Balashov, Jason R. Stagno, Jennifer M. Wang, Brigitte Schobert, Eleonora S. Imasheva, Janos K. Lanyi
Publikováno v:
Proceedings of the National Academy of Sciences. 105:16561-16565
Homologous to bacteriorhodopsin and even more to proteorhodopsin, xanthorhodopsin is a light-driven proton pump that, in addition to retinal, contains a noncovalently bound carotenoid with a function of a light-harvesting antenna. We determined the s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de37651ba773741c43ed6cb955bda612
https://doi.org/10.1073/pnas.0807162105
https://doi.org/10.1073/pnas.0807162105
Autor:
Jennifer M. Wang, Mordechai Sheves, Elena Smolensky, Sergei P. Balashov, Eleonora S. Imasheva, Janos K. Lanyi
Publikováno v:
Photochemistry and Photobiology. 84:977-984
Xanthorhodopsin is a light-driven proton pump in the extremely halophilic bacterium Salinibacter ruber. Its unique feature is that besides retinal it has a carotenoid, salinixanthin, with a light harvesting function. Tight and specific binding of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a02ed7589973146f40167260208f090e
https://doi.org/10.1111/j.1751-1097.2008.00337.x
https://doi.org/10.1111/j.1751-1097.2008.00337.x
Autor:
Takayuki Abe, Sergei P. Balashov, Takashi Kikukawa, Chabita K. Saha, Eleonora S. Imasheva, Naoki Kamo, Dmitry Zaslavsky, Robert B. Gennis
Publikováno v:
Photochemistry and Photobiology. 84:880-888
Pharaonis phoborhodopsin (ppR), a negative phototaxis receptor of Natronomonas pharaonis, undergoes photocycle similar to the light-driven proton pump bacteriorhodopsin (BR), but the turnover rate is much slower due to much longer lifetimes of the M
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a00bb1703095f706aa717b3f22bffa2e
https://doi.org/10.1111/j.1751-1097.2008.00318.x
https://doi.org/10.1111/j.1751-1097.2008.00318.x
Publikováno v:
Biochemistry. 45:10998-11004
In xanthorhodopsin, a retinal protein-carotenoid complex of Salinibacter ruber, the carotenoid salinixanthin functions as a light-harvesting antenna in supplying additional excitation energy for retinal isomerization and proton transport. Another ret
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29085e72bc030aee72596422da2eb9e9
https://doi.org/10.1021/bi061098i
https://doi.org/10.1021/bi061098i