How water-mediated hydrogen bonds affect chlorophyll a/b selectivity in Water-Soluble Chlorophyll Protein
| Autor: | Alessandro Agostini, Elena Meneghin, Lucas Gewehr, Danilo Pedron, Daniel M. Palm, Donatella Carbonera, Harald Paulsen, Elmar Jaenicke, Elisabetta Collini |
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| Rok vydání: | 2019 |
| Předmět: |
Chlorophyll
0106 biological sciences Protein Conformation lcsh:Medicine macromolecular substances Crystallography X-Ray Spectrum Analysis Raman Biochemistry 01 natural sciences Article 03 medical and health sciences Biophysical chemistry polycyclic compounds Photosynthesis lcsh:Science Plant Proteins X-ray crystallography 030304 developmental biology 0303 health sciences Multidisciplinary Chlorophyll A lcsh:R food and beverages Water Hydrogen Bonding Chemical biology Solubility Brassicaceae Raman spectroscopy lcsh:Q 010606 plant biology & botany |
| Zdroj: | Scientific Reports Scientific Reports, Vol 9, Iss 1, Pp 1-10 (2019) |
| ISSN: | 2045-2322 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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