ArticleProceedings of the National Academy of Sciences of the United States of America2017
Photoactivation mechanism of a carotenoid-based photoreceptor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 79 citations in OpenAlex.
- De novo coassembly of functional chlorophyll- and carotenoid-protein complexes inScience advances · 2026Article
- Atomistic simulations reveal the photoactivation mechanism of a carotenoid-binding photoreceptor.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Protein/linker dynamics facilitates the structural adaptation of the orange carotenoid protein in cyanobacterial photoprotection: a neutron scattering study.Photosynthesis research · 2026Article
- A Bright and Dynamic Future in Structural Biology.Advances in experimental medicine and biology · 2026Review
- Phycobilisome core architecture influences photoprotective quenching by the Orange Carotenoid Protein.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Photoacclimation strategies in cyanobacterial photosynthesis under dynamic light environments: implications in growth, fitness, and biotechnological applications.Frontiers in microbiology · 2025Review
- Article
- Solution Structures of Two Different FRP-OCP Complexes as Revealed via SEC-SANS.International journal of molecular sciences · 2024Article
- How orange carotenoid protein controls the excited state dynamics of canthaxanthin.Chemical science · 2023Article
- Orange Carotenoid Protein in Mesoporous Silica: A New System towards the Development of Colorimetric and Fluorescent Sensors for pH and Temperature.Micromachines · 2023Article
- Light activation of Orange Carotenoid Protein reveals bicycle-pedal single-bond isomerization.Nature communications · 2022Article
- Oligomerization processes limit photoactivation and recovery of the orange carotenoid protein.Biophysical journal · 2022Article
- A favorable path to domain separation in the orange carotenoid protein.Protein science : a publication of the Protein Society · 2022Article
- Role of hydrogen bond alternation and charge transfer states in photoactivation of the Orange Carotenoid Protein.Communications biology · 2021Article
- Molecular Mechanisms of Activation in the Orange Carotenoid Protein Revealed by Molecular Dynamics.Journal of the American Chemical Society · 2020Article
- An automated platform forIUCrJ · 2020Article
- Comparative ultrafast spectroscopy and structural analysis of OCP1 and OCP2 from Tolypothrix.Biochimica et biophysica acta. Bioenergetics · 2020Article
- Ultrafast Structural Changes Decomposed from Serial Crystallographic Data.The journal of physical chemistry letters · 2019Article
- Structural basis of molecular logic OR in a dual-sensor histidine kinase.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- X-ray radiolytic labeling reveals the molecular basis of orange carotenoid protein photoprotection and its interactions with fluorescence recovery protein.The Journal of biological chemistry · 2019Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Photoprotection is essential for efficient photosynthesis. Cyanobacteria have evolved a unique photoprotective mechanism mediated by a water-soluble carotenoid-based photoreceptor known as orange carotenoid protein (OCP). OCP undergoes large conformational changes in response to intense blue light, and the photoactivated OCP facilitates dissipation of excess energy via direct interaction with allophycocyanins at the phycobilisome core. However, the structural events leading up to the OCP photoactivation remain elusive at the molecular level. Here we present direct observations of light-induced structural changes in OCP captured by dynamic crystallography. Difference electron densities between the dark and illuminated states reveal widespread and concerted atomic motions that lead to altered protein-pigment interactions, displacement of secondary structures, and domain separation. Based on these crystallographic observations together with site-directed mutagenesis, we propose a molecular mechanism for OCP light perception, in which the photochemical property of a conjugated carbonyl group is exploited. We hypothesize that the OCP photoactivation starts with keto-enol tautomerization of the essential 4-keto group in the carotenoid, which disrupts the strong hydrogen bonds between the bent chromophore and the protein moiety. Subsequent structural changes trapped in the crystal lattice offer a high-resolution glimpse of the initial molecular events as OCP begins to transition from the orange-absorbing state to the active red-absorbing state.
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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.