ArticleThe journal of physical chemistry. B2021
On the Role of the Conserved Histidine at the Chromophore Isomerization Site in Phytochromes.
Article in The journal of physical chemistry. B, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Proton-Coupled Chromophore and Protein Structural Changes Control Phytochrome Activation.Biochemistry · 2026Article
- Photoisomerization of phytochrome's chromophore: a vibrational spectroscopic view on the primary ground state processes.RSC advances · 2025Article
- Pr and Pfr structures of plant phytochrome A.Nature communications · 2025Article
- Development of bright red-shifted miRFP704nano using structural analysis of miRFPnano proteins.Protein science : a publication of the Protein Society · 2023Article
- Vibrational Spectroscopy of Phytochromes.Biomolecules · 2023Review
- Conserved histidine and tyrosine determine spectral responses through the water network in Deinococcus radiodurans phytochrome.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022Article
- The structural effect between the output module and chromophore-binding domain is a two-way street via the hairpin extension.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Phytochromes are sensory photoreceptors that use light to drive protein structural changes, which in turn trigger physiological reaction cascades. The process starts with a double-bond photoisomerization of the linear methine-bridged tetrapyrrole chromophore in the photosensory core module. The molecular mechanism of the photoconversion depends on the structural and electrostatic properties of the chromophore environment, which are highly conserved in related phytochromes. However, the specific role of individual amino acids is yet not clear. A histidine in the vicinity of the isomerization site is highly conserved and almost invariant among all phytochromes. The present study aimed at analyzing its role by taking advantage of a myxobacterial phytochrome SaBphP1 from
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Registered trials
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