ArticleThe Journal of biological chemistry2011
Role of bulk water in hydrolysis of the rhodopsin chromophore.
Article in The Journal of biological chemistry, 2011. 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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Who cites it
36 citing papers in PubMed, 64 citations in OpenAlex.
- Conformational signatures of native ligand and pharmacochaperone binding in rhodopsin.Structure (London, England : 1993) · 2026Article
- Visual cycle-derived bisretinoids as endogenous natural products: enzyme-free formation, photochemical reactivity, and retinal degeneration.Natural product reports · 2026Review
- Structure of human green cone opsin yields insights into mechanisms underlying the rapid decay of its active, signaling state.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Roles of Hydration in Protein-Ligand Binding: Passive or Active Participant?The journal of physical chemistry. A · 2025Article
- Vitamin A supply in the eye and establishment of the visual cycle.Current topics in developmental biology · 2025Review
- Active state structures of a bistable visual opsin bound to G proteins.Nature communications · 2024Article
- A short story on how chromophore is hydrolyzed from rhodopsin for recycling.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Review
- Molecular basis of ligand selectivity for melatonin receptors.RSC advances · 2023Article
- New insights into the molecular mechanism of rhodopsin retinitis pigmentosa from the biochemical and functional characterization of G90V, Y102H and I307N mutations.Cellular and molecular life sciences : CMLS · 2022Article
- Rhodopsin as a Molecular Target to Mitigate Retinitis Pigmentosa.Advances in experimental medicine and biology · 2022Review
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- Molecular components affecting ocular carotenoid and retinoid homeostasis.Progress in retinal and eye research · 2021Review
- Exploring the Retinal Binding Cavity of Archaerhodopsin-3 by Replacing the Retinal Chromophore With a Dimethyl Phenylated Derivative.Frontiers in molecular biosciences · 2021Article
- Structural basis for ligand modulation of the CCR2 conformational landscape.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- Photocyclic behavior of rhodopsin induced by an atypical isomerization mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Article
- Utilization of Dioxygen by Carotenoid Cleavage Oxygenases.The Journal of biological chemistry · 2015Article
- Conformational selection and equilibrium governs the ability of retinals to bind opsin.The Journal of biological chemistry · 2015Article
- The G protein-coupled receptor rhodopsin: a historical perspective.Methods in molecular biology (Clifton, N.J.) · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Rhodopsin (Rho) is a prototypical G protein-coupled receptor that changes from an inactive conformational state to a G protein-activating state as a consequence of its retinal chromophore isomerization, 11-cis-retinal → all-trans-retinal. The photoisomerized chromophore covalently linked to Lys(296) by a Schiff base is subsequently hydrolyzed, but little is known about this reaction. Recent research indicates a significant role for tightly bound transmembrane water molecules in the Rho activation process. Atomic structures of Rho and hydroxyl radical footprinting reveal ordered waters within Rho transmembrane helices that are located close to highly conserved and functionally important receptor residues, forming a hydrogen bond network. Using (18)O-labeled H(2)O, we now report that water from bulk solvent, but not tightly bound water, is involved in the hydrolytic release of chromophore upon Rho activation by light. Moreover, small molecules (and presumably, water) enter the Rho structure from the cytoplasmic side of the membrane. Thus, this work indicates two distinct origins of water vital for Rho function.
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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.