Results 21 to 30 of about 634,170 (178)

Microbial rhodopsins on leaf surfaces of terrestrial plants [PDF]

Environmental Microbiology, 2011
Author Posting. © The Author(s), 2011. This is the author's version of the work. It is posted here by permission of John Wiley & Sons for personal use, not for redistribution. The definitive version was published in Environmental Microbiology 14 (2012):
Anton F. Post, Post, Anton F., Spudich, John L., Nof Atamna-Ismaeel, Atamna-Ismaeel, Nof, Beja, Oded, David Iluz, Omri M. Finkel, Spudich, J L, Itai Sharon, Julia A. Vorholt, Sharon, I, Christian von Mering, Finkel, Omri M., Belkin, S, Fabian Glaser, Glaser, F, Iluz, David, Glaser, Fabian, Oded Béjà, Atamna-Ismaeel, N, von Mering, C; https://orcid.org/, Vorholt, J A, von Mering, Christian, Finkel, O M, Post, A F, Vorholt, Julia A., Béjà, O, Schneider, R, Iluz, D, Belkin, Shimshon, Sharon, Itai, Schneider, Ron, John L. Spudich, Ron Schneider, Shimshon Belkin   +35 more
core   +6 more sources

Production and Structural Dynamics of Microbial Rhodopsins [PDF]

, 2019
Rhodopsins are a family of membrane proteins that are found in a wide range of organisms and provide them with the ability to sense and react to light.
Wickstrand, Cecilia
core   +4 more sources

Introduction of Session 7, “Functional diversity and evolution in microbial rhodopsins” [PDF]

Biophysics and Physicobiology, 2023
Takeshi Murata
doaj   +2 more sources

Omega Rhodopsins: A Versatile Class of Microbial Rhodopsins. [PDF]

J Microbiol Biotechnol, 2020
Microbial rhodopsins are a superfamily of photoactive membrane proteins with covalently bound retinal cofactor. Isomerization of the retinal chromophore upon absorption of a photon triggers conformational changes of the protein to function as ion pumps or sensors.
Kwon SK, Jun SH, Kim JF.
europepmc   +4 more sources

Unique Photochemistry Observed in a New Microbial Rhodopsin

The Journal of Physical Chemistry Letters, 2019
Light energy is first captured in animal and microbial rhodopsins by ultrafast photoisomerization, whose relaxation accompanies protein structural changes for each function.
Hideki Kandori (534378), Kota Katayama (1355721), Oded Béjà (5597627), Keiichi Inoue (466261), Chihiro Kataoka (7296485)   +4 more
core   +3 more sources

A Detailed View on the (Re)Isomerization Dynamics in Microbial Rhodopsins Using Complementary Near-UV and IR Readouts [PDF]

Angewandte Chemie - International Edition
Joachim Heberle, Kirill Kovalev, Clemens Glaubitz   +2 more
exaly   +2 more sources

Scramblase activity of proteorhodopsin confers physiological advantages to Escherichia coli in the absence of light

iScience, 2023
Summary: Microbial rhodopsins are widely distributed in the aqua-ecosystem due to their simple structure and multifaceted functions. Conventionally, microbial rhodopsins are considered to be exclusively light active.
Jiayu Fang, Yanping Zhang, Taicheng Zhu, Yin Li   +3 more
doaj   +1 more source

A Distinct Abundant Group of Microbial Rhodopsins Discovered Using Functional Metagenomics [PDF]

Nature, 2018
Oded Béjà, Masae Konno, Ryoko Nakamura
exaly   +2 more sources

Near-Infrared Activation of Sensory Rhodopsin II Mediated by NIR-to-Blue Upconversion Nanoparticles

Frontiers in Molecular Biosciences, 2022
Direct optical activation of microbial rhodopsins in deep biological tissue suffers from ineffective light delivery because visible light is strongly scattered and absorbed.
Momo Yaguchi, Xiaodan Jia, Ramona Schlesinger, Xiue Jiang, Kenichi Ataka, Joachim Heberle   +5 more
doaj   +1 more source

Mechanism divergence in microbial rhodopsins. [PDF]

Biochim Biophys Acta, 2014
A fundamental design principle of microbial rhodopsins is that they share the same basic light-induced conversion between two conformers. Alternate access of the Schiff base to the outside and to the cytoplasm in the outwardly open "E" conformer and cytoplasmically open "C" conformer, respectively, combined with appropriate timing of pKa changes ...
Spudich JL, Sineshchekov OA, Govorunova EG.   +2 more
europepmc   +3 more sources