Results 131 to 140 of about 641,669 (159)

Photochemistry of the Retinal Chromophore in Microbial Rhodopsins

The Journal of Physical Chemistry B, 2023
Microbial rhodopsins are photoreceptive membrane proteins of microorganisms that express diverse photobiological functions. All-trans-retinylidene Schiff base, the so-called all-trans-retinal, is a chromophore of microbial rhodopsins, which captures photons. It isomerizes into the 13-cis form upon photoexcitation.
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Optogenetic control of plant growth by a microbial rhodopsin

Nature Plants, 2021
While rhodopsin-based optogenetics has revolutionized neuroscience1,2, poor expression of opsins and the absence of the essential cofactor all-trans-retinal has complicated the application of rhodopsins in plants. Here, we demonstrate retinal production in plants and improved rhodopsin targeting for green light manipulation of plant cells using the ...
Yang Zhou, Meiqi Ding, Shiqiang Gao, Jing Yu-Strzelczyk, Markus Krischke, Xiaodong Duan, Jana Leide, Markus Riederer, Martin J. Mueller, Rainer Hedrich, Kai R. Konrad, Georg Nagel   +11 more
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Molecular Biology of Microbial Rhodopsins

2022
Research on type 1 rhodopsins spans now a history of 50 years. Originally, just archaeal ion pumps and sensors have been discovered. However, with modern genetic techniques and gene sequencing tools, more and more proteins were identified in all kingdoms of life. Spectroscopic and other biophysical studies revealed quite diverse functions.
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Solid-State NMR Spectroscopy on Microbial Rhodopsins

2022
Microbial rhodopsins represent the most abundant phototrophic systems known today. A similar molecular architecture with seven transmembrane helices and a retinal cofactor linked to a lysine in helix 7 enables a wide range of functions including ion pumping, light-controlled ion channel gating, or sensing.
Clara Nassrin, Kriebel, Johanna, Becker-Baldus, Clemens, Glaubitz   +2 more
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The multitalented microbial sensory rhodopsins

Trends in Microbiology, 2006
Sensory rhodopsins are photoactive, membrane-embedded seven-transmembrane helix receptors that use retinal as a chromophore. They are widespread in the microbial world in each of the three domains of life: Archaea, Bacteria and Eukarya. A striking characteristic of these photoreceptors is their different modes of signaling in different organisms ...
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Measuring Membrane Voltage with Microbial Rhodopsins

2013
Membrane voltage (Vm) is a fundamental biological parameter that is essential for neuronal communication, cardiac activity, transmembrane transport, regulation of signaling, and bacterial motility. Optical measurements of Vm promise new insights into how voltage propagates within and between cells, but effective optical contrast agents have been ...
Adam E, Cohen, Daniel R, Hochbaum
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Photoreversible Reactions of Visual and Microbial Rhodopsins

Biochemistry (Moscow)
The review discusses experimental findings and theoretical studies of photoreversible transformations of retinal-containing proteins (rhodopsins). Understanding these processes is essential for elucidating the mechanisms of photochemical and conformational transformations of these proteins.
Mikhail A, Ostrovsky, Olga A, Smitienko, Tatiana B, Feldman   +2 more
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Microbial rhodopsins: functional versatility and genetic mobility

Trends in Microbiology, 2006
The type 1 (microbial) rhodopsins are a diverse group of photochemically reactive proteins that span the three domains of life. Their broad phylogenetic distribution has motivated conjecture that rhodopsin-like functionality was present in the last common ancestor of all life.
Adrian K, Sharma, John L, Spudich, W Ford, Doolittle   +2 more
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Microbial Sensory Rhodopsins: Photochemistry and Function

Israel Journal of Chemistry, 1995
AbstractThe review covers recent progress on microbial sensory rhodopsins, visual pigment‐like retinylidene photoreceptors that function in phototaxis by archaeons, such asHalobacterium salinarium, and by unicellular eukaryotic algae, such asChlamydomonas reinhardtii.Six demonstrably different sensory rhodopsins are known in halophilic archaea.
John L. Spudich, David N. Zacks, Roberto A. Bogomolni   +2 more
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Structural insights into retinal-free microbial rhodopsins

Structure
Rhodopsins typically harness light energy through the covalently bound retinal cofactor. However, some rhodopsins have lost this ability during evolution. In this issue of Structure, Kovalev et al.1 present the cryo-electron microscopy (cryo-EM) structure of a retinal-free flotillin-associated rhodopsin (FArhodopsin), providing new insights into their ...
Zhenmei, Xu, Yuanzheng, He
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