Photoprotective conformational dynamics of photosynthetic light-harvesting proteins.
Free-energy landscapes
Photoprotection
Photosynthetic light harvesting
Single-molecule spectroscopy
Journal
Biochimica et biophysica acta. Bioenergetics
ISSN: 1879-2650
Titre abrégé: Biochim Biophys Acta Bioenerg
Pays: Netherlands
ID NLM: 101731706
Informations de publication
Date de publication:
01 04 2022
01 04 2022
Historique:
received:
01
11
2021
revised:
25
01
2022
accepted:
15
02
2022
pubmed:
25
2
2022
medline:
19
4
2022
entrez:
24
2
2022
Statut:
ppublish
Résumé
Under high light conditions, excess energy can damage the machinery of oxygenic photosynthesis. Plants have evolved a series of photoprotective processes, including conformational changes of the light-harvesting complexes that activate dissipation of energy as heat. In this mini-review, we will summarize our recent work developing and applying single-molecule methods to investigate the conformational states of the light-harvesting complexes. Through these measurements, we identified dissipative conformations and how they depend on conditions that mimic high light. Our studies revealed an equilibrium between the light-harvesting and dissipative conformations, and that the nature of the equilibrium varies with cellular environment, between proteins, and between species. Finally, we conclude with an outlook on open questions and implications for photosynthetic yields.
Identifiants
pubmed: 35202576
pii: S0005-2728(22)00012-3
doi: 10.1016/j.bbabio.2022.148543
pii:
doi:
Substances chimiques
Light-Harvesting Protein Complexes
0
Tumor Necrosis Factor Ligand Superfamily Member 14
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
148543Informations de copyright
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