ArticleBiophysical journal2015
The Signaling State of Orange Carotenoid Protein.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 99 citations in OpenAlex.
- No-tillage systems promote bacterial photosynthetic gene expression in low carbon, semi-arid surface soils.Applied and environmental microbiology · 2025Article
- Two-Photon-Driven Photoprotection Mechanism in Echinenone-Functionalized Orange Carotenoid Protein.Journal of the American Chemical Society · 2025Article
- Photoacclimation strategies in cyanobacterial photosynthesis under dynamic light environments: implications in growth, fitness, and biotechnological applications.Frontiers in microbiology · 2025Review
- How electron tunneling and uphill excitation energy transfer support photochemistry in Halomicronema hongdechloris.Photosynthesis research · 2024Article
- Adaptation processes inFrontiers in plant science · 2024Review
- How orange carotenoid protein controls the excited state dynamics of canthaxanthin.Chemical science · 2023Article
- The role of the local environment on the structural heterogeneity of carotenoid β-ionone rings.Photosynthesis research · 2023Article
- Parameterization of a single H-bond in Orange Carotenoid Protein by atomic mutation reveals principles of evolutionary design of complex chemical photosystems.Frontiers in molecular biosciences · 2023Article
- Is orange carotenoid protein photoactivation a single-photon process?Biophysical reports · 2022Article
- A favorable path to domain separation in the orange carotenoid protein.Protein science : a publication of the Protein Society · 2022Article
- Integrated Structural Studies for Elucidating Carotenoid-Protein Interactions.Advances in experimental medicine and biology · 2022Article
- Role of hydrogen bond alternation and charge transfer states in photoactivation of the Orange Carotenoid Protein.Communications biology · 2021Article
- Spectral Features of Canthaxanthin in HCP2. A QM/MM Approach.Molecules (Basel, Switzerland) · 2021Article
- Soluble Cyanobacterial Carotenoprotein as a Robust Antioxidant Nanocarrier and Delivery Module.Antioxidants (Basel, Switzerland) · 2020Article
- Probing of carotenoid-tryptophan hydrogen bonding dynamics in the single-tryptophan photoactive Orange Carotenoid Protein.Scientific reports · 2020Article
- Comparative ultrafast spectroscopy and structural analysis of OCP1 and OCP2 from Tolypothrix.Biochimica et biophysica acta. Bioenergetics · 2020Article
- Interdomain interactions reveal the molecular evolution of the orange carotenoid protein.Nature plants · 2019Article
- A genetically encoded fluorescent temperature sensor derived from the photoactive Orange Carotenoid Protein.Scientific reports · 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
- OCP-FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria.Nature communications · 2018Article
Corrections and comments
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Authors and funding
13 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Orange carotenoid protein (OCP) is the photoactive protein that is responsible for high light tolerance in cyanobacteria. We studied the kinetics of the OCP photocycle by monitoring changes in its absorption spectrum, intrinsic fluorescence, and fluorescence of the Nile red dye bound to OCP. It was demonstrated that all of these three methods provide the same kinetic parameters of the photocycle, namely, the kinetics of OCP relaxation in darkness was biexponential with a ratio of two components equal to 2:1 independently of temperature. Whereas the changes of the absorption spectrum of OCP characterize the geometry and environment of its chromophore, the intrinsic fluorescence of OCP reveals changes in its tertiary structure, and the fluorescence properties of Nile red indicate the exposure of hydrophobic surface areas of OCP to the solvent following the photocycle. The results of molecular-dynamics studies indicated the presence of two metastable conformations of 3'-hydroxyechinenone, which is consistent with characteristic changes in the Raman spectra. We conclude that rotation of the β-ionylidene ring in the C-terminal domain of OCP could be one of the first conformational rearrangements that occur during photoactivation. The obtained results suggest that the photoactivated form of OCP represents a molten globule-like state that is characterized by increased mobility of tertiary structure elements and solvent accessibility.
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