ArticleBiochemistry2016
Dramatic Domain Rearrangements of the Cyanobacterial Orange Carotenoid Protein upon Photoactivation.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 72 citations in OpenAlex.
- 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
- Photoacclimation strategies in cyanobacterial photosynthesis under dynamic light environments: implications in growth, fitness, and biotechnological applications.Frontiers in microbiology · 2025Review
- The Orange Carotenoid Protein Triggers Cyanobacterial Photoprotection by Quenching Bilins via a Structural Switch of Its Carotenoid.Journal of the American Chemical Society · 2024Article
- Solution Structures of Two Different FRP-OCP Complexes as Revealed via SEC-SANS.International journal of molecular sciences · 2024Article
- Color-Tuning Mechanism of the Lit Form of Orange Carotenoid Protein.Molecules and cells · 2023Article
- 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
- Molecular Mechanisms of Activation in the Orange Carotenoid Protein Revealed by Molecular Dynamics.Journal of the American Chemical Society · 2020Article
- Interdomain interactions reveal the molecular evolution of the orange carotenoid protein.Nature plants · 2019Article
- Phycobilisomes Harbor FNRmBio · 2019Article
- Single-molecule trapping and spectroscopy reveals photophysical heterogeneity of phycobilisomes quenched by Orange Carotenoid Protein.Nature communications · 2019Article
- Photoactivation Mechanism, Timing of Protein Secondary Structure Dynamics and Carotenoid Translocation in the Orange Carotenoid Protein.Journal of the American Chemical Society · 2019Article
- Site, trigger, quenching mechanism and recovery of non-photochemical quenching in cyanobacteria: recent updates.Photosynthesis research · 2018Review
- Photoprotective, excited-state quenching mechanisms in diverse photosynthetic organisms.The Journal of biological chemistry · 2018Review
- Interaction of the signaling state analog and the apoprotein form of the orange carotenoid protein with the fluorescence recovery protein.Photosynthesis research · 2018Article
- The photocycle of orange carotenoid protein conceals distinct intermediates and asynchronous changes in the carotenoid and protein components.Scientific reports · 2017Article
- Paralogs of the C-Terminal Domain of the Cyanobacterial Orange Carotenoid Protein Are Carotenoid Donors to Helical Carotenoid Proteins.Plant physiology · 2017Article
- Coupled rows of PBS cores and PSII dimers in cyanobacteria: symmetry and structure.Photosynthesis research · 2017Article
- Photoactivation mechanism of a carotenoid-based photoreceptor.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Photosynthetic cyanobacteria make important contributions to global carbon and nitrogen budgets. A protein known as the orange carotenoid protein (OCP) protects the photosynthetic apparatus from damage by dissipating excess energy absorbed by the phycobilisome, the major light-harvesting complex in many cyanobacteria. OCP binds one carotenoid pigment, but the color of this pigment depends on conditions. It is orange in the dark and red when exposed to light. We modified the orange and red forms of OCP by using isotopically coded cross-linking agents and then analyzed the structural features by using liquid chromatography and tandem mass spectrometry. Unequivocal cross-linking pairs uniquely detected in red OCP indicate that, upon photoactivation, the OCP N-terminal domain (NTD) and C-terminal domain (CTD) reorient relative to each other. Our data also indicate that the intrinsically unstructured loop connecting the NTD and CTD not only is involved in the interaction between the two domains in orange OCP but also, together with the N-terminal extension, provides a structural buffer system facilitating an intramolecular breathing motion of the OCP, thus helping conversion back and forth from the orange to red form during the OCP photocycle. These results have important implications for understanding the molecular mechanism of action of cyanobacterial photoprotection.
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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.