Engineering a pH-regulated switch in the major light-harvesting complex of plants (LHCII): proof of principle
| Autor: | Roberta Croce, Alberto Natali, Nicoletta Liguori |
|---|---|
| Přispěvatelé: | Biophysics Photosynthesis/Energy, LaserLaB - Energy |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
Models
Molecular Protein Conformation alpha-Helical 0301 basic medicine Conformational change Light LHCSR Arabidopsis Light-Harvesting Protein Complexes Gene Expression Chlamydomonas reinhardtii Photochemistry Thylakoids Light-harvesting complex Materials Chemistry Transgenes Cloning Molecular Photosynthesis LIGHT-HARVESTING biology Chemistry Hydrogen-Ion Concentration Recombinant Proteins Surfaces Coatings and Films PH REGULATION Thylakoid Thermodynamics Genetic Engineering Protein Binding LHCII Allosteric regulation 03 medical and health sciences Escherichia coli Protein Interaction Domains and Motifs Amino Acid Sequence SDG 7 - Affordable and Clean Energy Physical and Theoretical Chemistry Binding Sites Sequence Homology Amino Acid PHOTOPROTECTION Pigments Biological biology.organism_classification Kinetics 030104 developmental biology Photoprotection Mutation Photosynthetic membrane Sequence Alignment QUENCHING |
| Zdroj: | Journal of Physical Chemistry B, 120(49), 12531-12535. American Chemical Society Liguori, N, Natali, A & Croce, R 2016, ' Engineering a pH-regulated switch in the major light-harvesting complex of plants (LHCII): proof of principle ', Journal of Physical Chemistry B, vol. 120, no. 49, pp. 12531-12535 . https://doi.org/10.1021/acs.jpcb.6b11541 |
| ISSN: | 1520-6106 |
| Popis: | Under excess light, photosynthetic organisms employ feedback mechanisms to avoid photodamage. Photoprotection is triggered by acidification of the lumen of the photosynthetic membrane following saturation of the metabolic activity. A low pH triggers thermal dissipation of excess absorbed energy by the light-harvesting complexes (LHCs). LHCs are not able to sense pH variations, and their switch to a dissipative mode depends on stress-related proteins and allosteric cofactors. In green algae the trigger is the pigment–protein complex LHCSR3. Its C-terminus is responsible for a pH-driven conformational change from a light-harvesting to a quenched state. Here, we show that by replacing the C-terminus of the main LHC of plants with that of LHCSR3, it is possible to regulate its excited-state lifetime solely via protonation, demonstrating that the protein template of LHCs can be modified to activate reversible quenching mechanisms independent of external cofactors and triggers. |
| Databáze: | OpenAIRE |
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