ArticleFrontiers in molecular biosciences2015
Conformational heterogeneity of the Pfr chromophore in plant and cyanobacterial phytochromes.
Article in Frontiers in molecular biosciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Proton-Coupled Chromophore and Protein Structural Changes Control Phytochrome Activation.Biochemistry · 2026Article
- PHY domain governs structural and photochemical fidelity in the far-red-absorbing state of phytochromes.Frontiers in molecular biosciences · 2026Article
- Vibrational Spectroscopy of Phytochromes.Biomolecules · 2023Review
- Enhancing the Inhomogeneous Photodynamics of Canonical Bacteriophytochrome.The journal of physical chemistry. B · 2022Article
- Ultrafast Photoconversion Dynamics of the Knotless PhytochromeInternational journal of molecular sciences · 2021Article
- Modulation of Structural Heterogeneity Controls Phytochrome Photoswitching.Biophysical journal · 2020Article
- 3D Structures of Plant Phytochrome A as Pr and Pfr From Solid-State NMR: Implications for Molecular Function.Frontiers in plant science · 2018Article
- From photon to signal in phytochromes: similarities and differences between prokaryotic and plant phytochromes.Journal of plant research · 2016Review
- NMR chemical shift pattern changed by ammonium sulfate precipitation in cyanobacterial phytochrome Cph1.Frontiers in molecular biosciences · 2015Article
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13 authors.
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Abstract
Phytochromes are biological photoreceptors that can be reversibly photoconverted between a dark and photoactivated state. The underlying reaction sequences are initiated by the photoisomerization of the tetrapyrrole cofactor, which in plant and cyanobacterial phytochromes are a phytochromobilin (PΦB) and a phycocyanobilin (PCB), respectively. The transition between the two states represents an on/off-switch of the output module activating or deactivating downstream physiological processes. In addition, the photoactivated state, i.e., Pfr in canonical phytochromes, can be thermally reverted to the dark state (Pr). The present study aimed to improve our understanding of the specific reactivity of various PΦB- and PCB-binding phytochromes in the Pfr state by analysing the cofactor structure by vibrational spectroscopic techniques. Resonance Raman (RR) spectroscopy revealed two Pfr conformers (Pfr-I and Pfr-II) forming a temperature-dependent conformational equilibrium. The two sub-states-found in all phytochromes studied, albeit with different relative contributions-differ in structural details of the C-D and A-B methine bridges. In the Pfr-I sub-state the torsion between the rings C and D is larger by ca. 10° compared to Pfr-II. This structural difference is presumably related to different hydrogen bonding interactions of ring D as revealed by time-resolved IR spectroscopic studies of the cyanobacterial phytochrome Cph1. The transitions between the two sub-states are evidently too fast (i.e., nanosecond time scale) to be resolved by NMR spectroscopy which could not detect a structural heterogeneity of the chromophore in Pfr. The implications of the present findings for the dark reversion of the Pfr state are discussed.
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