ReviewBiochimica et biophysica acta2014
Mechanism divergence in microbial rhodopsins.
Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
36 citing papers in PubMed, 69 citations in OpenAlex.
- Surface Density-Dependent Interactions between Photoactivated Sensory Rhodopsin 2 and Its Transducer.ACS omega · 2026Article
- A second photoactivatable state of the anion-conducting channelrhodopsin GtACR1 empowers persistent activity.Communications biology · 2025Article
- Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography.Nature communications · 2025Article
- Actinorhodopsin: an efficient and robust light-driven proton pump for bionanotechnological applications.Scientific reports · 2025Article
- Structural insights into light-gating of potassium-selective channelrhodopsin.Nature communications · 2025Article
- KInternational journal of molecular sciences · 2023Article
- Ion-transporting mechanism in microbial rhodopsins: Mini-review relating to the session 5 at the 19th International Conference on Retinal Proteins.Biophysics and physicobiology · 2023Article
- Structural insights into light-driven anion pumping in cyanobacteria.Nature communications · 2022Article
- HwMR is a novel magnesium-associated protein.Biophysical journal · 2022Article
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- The Photoreaction of the Proton-Pumping Rhodopsin 1 From the Maize Pathogenic BasidiomyceteFrontiers in molecular biosciences · 2022Article
- Optical Switching Between Long-lived States of Opsin Transmembrane Voltage Sensors.Photochemistry and photobiology · 2021Article
- Gate-keeper of ion transport-a highly conserved helix-3 tryptophan in a channelrhodopsin chimera, C1C2/ChRWR.Biophysics and physicobiology · 2020Article
- Signal transduction in photoreceptor histidine kinases.Protein science : a publication of the Protein Society · 2019Review
- Functional importance of the oligomer formation of the cyanobacterial HScientific reports · 2019Article
- Protein Activity of the Fusarium fujikuroi Rhodopsins CarO and OpsA and Their Relation to Fungus-Plant Interaction.International journal of molecular sciences · 2018Article
- Microbial Rhodopsins: Diversity, Mechanisms, and Optogenetic Applications.Annual review of biochemistry · 2017Review
- Complex Photochemistry within the Green-Absorbing Channelrhodopsin ReaChR.Biophysical journal · 2017Article
- New Insights on Signal Propagation by Sensory Rhodopsin II/Transducer Complex.Scientific reports · 2017Article
- Molecular properties of a DTD channelrhodopsin fromBiophysics and physicobiology · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
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 controlling Schiff base proton release and uptake make the proton path through the pumps vectorial. Phototaxis receptors in prokaryotes, sensory rhodopsins I and II, have evolved new chemical processes not found in their proton pump ancestors, to alter the consequences of the conformational change or modify the change itself. Like proton pumps, sensory rhodopsin II undergoes a photoinduced E→C transition, with the C conformer a transient intermediate in the photocycle. In contrast, one light-sensor (sensory rhodopsin I bound to its transducer HtrI) exists in the dark as the C conformer and undergoes a light-induced C→E transition, with the E conformer a transient photocycle intermediate. Current results indicate that algal phototaxis receptors channelrhodopsins undergo redirected Schiff base proton transfers and a modified E→C transition which, contrary to the proton pumps and other sensory rhodopsins, is not accompanied by the closure of the external half-channel. The article will review our current understanding of how the shared basic structure and chemistry of microbial rhodopsins have been modified during evolution to create diverse molecular functions: light-driven ion transport and photosensory signaling by protein-protein interaction and light-gated ion channel activity. This article is part of a Special Issue entitled: Retinal Proteins - You can teach an old dog new tricks.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.