Energy dissipation efficiency in the CP43 assembly intermediate complex of photosystem II.


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 08 2023
Historique:
received: 10 02 2023
revised: 10 04 2023
accepted: 20 04 2023
medline: 15 6 2023
pubmed: 6 5 2023
entrez: 5 5 2023
Statut: ppublish

Résumé

Photosystem II in oxygenic organisms is a large membrane bound rapidly turning over pigment protein complex. During its biogenesis, multiple assembly intermediates are formed, including the CP43-preassembly complex (pCP43). To understand the energy transfer dynamics in pCP43, we first engineered a His-tagged version of the CP43 in a CP47-less strain of the cyanobacterium Synechocystis 6803. Isolated pCP43 from this engineered strain was subjected to advanced spectroscopic analysis to evaluate its excitation energy dissipation characteristics. These included measurements of steady-state absorption and fluorescence emission spectra for which correlation was tested with Stepanov relation. Comparison of fluorescence excitation and absorptance spectra determined that efficiency of energy transfer from β-carotene to chlorophyll a is 39 %. Time-resolved fluorescence images of pCP43-bound Chl a were recorded on streak camera, and fluorescence decay dynamics were evaluated with global fitting. These demonstrated that the decay kinetics strongly depends on temperature and buffer used to disperse the protein sample and fluorescence decay lifetime was estimated in 3.2-5.7 ns time range, depending on conditions. The pCP43 complex was also investigated with femtosecond and nanosecond time-resolved absorption spectroscopy upon excitation of Chl a and β-carotene to reveal pathways of singlet excitation relaxation/decay, Chl a triplet dynamics and Chl a → β-carotene triplet state sensitization process. The latter demonstrated that Chl a triplet in the pCP43 complex is not efficiently quenched by carotenoids. Finally, detailed kinetic analysis of the rise of the population of β-carotene triplets determined that the time constant of the carotenoid triplet sensitization is 40 ns.

Identifiants

pubmed: 37146928
pii: S0005-2728(23)00028-2
doi: 10.1016/j.bbabio.2023.148982
pii:
doi:

Substances chimiques

Photosystem II Protein Complex 0
Chlorophyll A YF5Q9EJC8Y
Chlorophyll 1406-65-1
Light-Harvesting Protein Complexes 0
beta Carotene 01YAE03M7J
Carotenoids 36-88-4

Types de publication

Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

148982

Informations de copyright

Copyright © 2023 Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Sandeep Biswas (S)

Department of Biology, Washington University, St. Louis, MO 63130, USA. Electronic address: sandeep.biswas@wustl.edu.

Dariusz M Niedzwiedzki (DM)

Center for Solar Energy and Energy Storage, Washington University, St. Louis, MO 63130, USA; Department of Energy, Environmental & Chemical Engineering, Washington University, St. Louis, MO 63130, USA. Electronic address: niedzwiedzki@wustl.edu.

Himadri B Pakrasi (HB)

Department of Biology, Washington University, St. Louis, MO 63130, USA. Electronic address: pakrasi@wustl.edu.

Articles similaires

Structural basis for molecular assembly of fucoxanthin chlorophyll

Koji Kato, Yoshiki Nakajima, Jian Xing et al.
1.00
Diatoms Photosystem I Protein Complex Chlorophyll Binding Proteins Cryoelectron Microscopy Light-Harvesting Protein Complexes
Water Quality Bays Environmental Monitoring Remote Sensing Technology Chlorophyll
Anthraquinones Kinetics Water Purification Adsorption Thermodynamics

Classifications MeSH