ArticleScientific reports2019
How water-mediated hydrogen bonds affect chlorophyll a/b selectivity in Water-Soluble Chlorophyll Protein.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Vibronic Coherence in a Minimal Pigment-Protein Complex Probed by Two-Dimensional Electronic-Vibrational Spectroscopy.The journal of physical chemistry. B · 2026Article
- The Role of H-Bonds in the Excited-State Properties of Multichromophoric Systems: Static and Dynamic Aspects.Molecules (Basel, Switzerland) · 2023Review
- Magnetophotoselection in the Investigation of Excitonically Coupled Chromophores: The Case of the Water-Soluble Chlorophyll Protein.Molecules (Basel, Switzerland) · 2022Article
- Primary donor triplet states of Photosystem I and II studied by Q-band pulse ENDOR spectroscopy.Photosynthesis research · 2022Article
- Protein Matrix Control of Reaction Center Excitation in Photosystem II.Journal of the American Chemical Society · 2020Article
- Accurate Computation of the Absorption Spectrum of ChlorophyllThe journal of physical chemistry. B · 2020Article
- The pigment binding behaviour of water-soluble chlorophyll protein (WSCP).Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2020Article
- How the Protein Environment Can Tune the Energy, the Coupling, and the Ultrafast Dynamics of Interacting Chlorophylls: The Example of the Water-Soluble Chlorophyll Protein.The journal of physical chemistry letters · 2020Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Water-Soluble Chlorophyll Protein (WSCP) of Brassicaceae is a remarkably stable tetrapyrrole-binding protein that, by virtue of its simple design, is an exceptional model to investigate the interactions taking place between pigments and their protein scaffold and how they affect the photophysical properties and the functionality of the complexes. We investigated variants of WSCP from Lepidium virginicum (Lv) and Brassica oleracea (Bo), reconstituted with Chlorophyll (Chl) b, to determine the mechanisms by which the different Chl binding sites control their Chl a/b specificities. A combined Raman and crystallographic investigation has been employed, aimed to characterize in detail the hydrogen-bond network involving the formyl group of Chl b. The study revealed a variable degree of conformational freedom of the hydrogen bond networks among the WSCP variants, and an unexpected mixed presence of hydrogen-bonded and not hydrogen-bonded Chls b in the case of the L91P mutant of Lv WSCP. These findings helped to refine the description of the mechanisms underlying the different Chl a/b specificities of WSCP versions, highlighting the importance of the structural rigidity of the Chl binding site in the vicinity of the Chl b formyl group in granting a strong selectivity to binding sites.
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