ArticlePhotosynthesis research2016
A comparative study of three signaling forms of the orange carotenoid protein.
Article in Photosynthesis research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 83 citations in OpenAlex.
- Protein/linker dynamics facilitates the structural adaptation of the orange carotenoid protein in cyanobacterial photoprotection: a neutron scattering study.Photosynthesis research · 2026Article
- Structure and quenching of a bundle-shaped phycobilisome.Science advances · 2025Article
- Engineering hydrogen bonding at tyrosine-201 in the orange carotenoid protein using halogenated analogues.Photosynthesis research · 2025Article
- Insights into the molecular mechanism of yellow cuticle coloration by a chitin-binding carotenoprotein in gregarious locusts.Communications biology · 2024Article
- How electron tunneling and uphill excitation energy transfer support photochemistry in Halomicronema hongdechloris.Photosynthesis research · 2024Article
- Adaptation processes inFrontiers in plant science · 2024Review
- Protein-Mediated Carotenoid Delivery Suppresses the Photoinducible Oxidation of Lipofuscin in Retinal Pigment Epithelial Cells.Antioxidants (Basel, Switzerland) · 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
- Probing Red Blood Cell Membrane Microviscosity Using Fluorescence Anisotropy Decay Curves of the Lipophilic Dye PKH26.International journal of molecular sciences · 2022Article
- Role of hydrogen bond alternation and charge transfer states in photoactivation of the Orange Carotenoid Protein.Communications biology · 2021Article
- Structural analysis of a new carotenoid-binding protein: the C-terminal domain homolog of the OCP.Scientific reports · 2020Article
- 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
- Thermal Inactivation of a Cold-Active Esterase PMGL3 Isolated from the Permafrost Metagenomic Library.Biomolecules · 2019Article
- 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
- Single-molecule trapping and spectroscopy reveals photophysical heterogeneity of phycobilisomes quenched by Orange Carotenoid Protein.Nature communications · 2019Article
- OCP-FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria.Nature communications · 2018Article
- Photoactivation and relaxation studies on the cyanobacterial orange carotenoid protein in the presence of copper ion.Photosynthesis research · 2018Article
- Interaction of the signaling state analog and the apoprotein form of the orange carotenoid protein with the fluorescence recovery protein.Photosynthesis research · 2018Article
Corrections and comments
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Authors and funding
15 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Orange carotenoid protein (OCP) is a water-soluble photoactive protein responsible for a photoprotective mechanism of nonphotochemical quenching in cyanobacteria. Under blue-green illumination, OCP converts from the stable orange into the signaling red quenching form; however, the latter form could also be obtained by chemical activation with high concentrations of sodium thiocyanate (NaSCN) or point mutations. In this work, we show that a single replacement of tryptophan-288, normally involved in protein-chromophore interactions, by alanine, results in formation of a new protein form, hereinafter referred to as purple carotenoid protein (PCP). Comparison of resonance Raman spectra of the native photoactivated red form, chemically activated OCP, and PCP reveals that carotenoid conformation is sensitive to the structure of the C-domain, implicating that the chromophore retains some interactions with this part of the protein in the active red form. Combination of differential scanning fluorimetry and picosecond time-resolved fluorescence anisotropy measurements allowed us to compare the stability of different OCP forms and to estimate relative differences in protein rotation rates. These results were corroborated by hydrodynamic analysis of proteins by dynamic light scattering and analytical size-exclusion chromatography, indicating that the light-induced conversion of the protein is accompanied by a significant increase in its size. On the whole, our data support the idea that the red form of OCP is a molten globule-like protein in which, however, interactions between the carotenoid and the C-terminal domain are preserved.
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