Structure and Energy Transfer of Algae Photosynthetic Antenna Organism Crystals

A special issue of Crystals (ISSN 2073-4352). This special issue belongs to the section "Organic Crystalline Materials".

Deadline for manuscript submissions: closed (15 November 2021) | Viewed by 3860

Special Issue Editors


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Guest Editor
Research director of Lab of Coastal Bioresources, Yantai Institute of Coastal Zone Research, Chunhui Rd 17,Laishan District, YanTai 264003,China
Interests: algae; light-harvesting system; structural biology; structural analysis technology; efficient energy transfer

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Guest Editor
School of physics, State Key Laboratory of OEMT, Sun Yat-sen University, Guangzhou 510275, China
Interests: photosynthesis; nonlinear optics; ultrafast dynamics

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Guest Editor
1. School of physics, State Key Laboratory of Optoelectronic Materials and Technologies, Sun Yat-sen University, Guangzhou 510275, China
2. Institute of Advanced Science Facilities, Shenzhen 518107, China
Interests: photosynthesis; photosynthetic antenna; energy transfer dynamics; time-resolved spectroscopy
Lab of Coastal Bioresources, Yantai Institute of Coastal Zone Research; Chunhui Rd 17,Laishan District, YanTai 264003,China
Interests: photosynthesis; algal light-harvesting complexes; light-harvesting protein; energy transfer dynamics; phycobiliprotein

Special Issue Information

Dear Colleagues,

Algal light-harvesting antenna complexes (LHCs) are vital apparatus for energy capture and transfer in algal photosynthesis. Different from higher plants, algal LHCs are more diverse in terms of pigment compositions and structures. Within the past years, structures the antenna complexes have been elucidated with the help of technological development in structural biology, and the structural analysis of algal LHC shows a development trend of "low resolution in situ / single particle structure - high resolution single particle / in situ structure". Furthermore, the antennas transfer the absorbed energy at almost 100% efficiency to the reaction centres that perform the photochemical electron transfer reactions required for the conversion of the light energy into useful and storable chemical energy. The antenna complex has a broad cross-section of absorption and mainly transfers the absorbed energy to photosystem II. They can, however, function as an antenna of photosystem I, and their composition can be altered as a result of changes in the environmental light quality.

We invite researchers to contribute to the Special Issue titled “Structure and Energy Transfer of Photosynthetic Antenna Organism Crystals”, which is intended to serve as a unique multidisciplinary forum covering broad aspects of structural and functional characteristics of the photosynthetic antenna complex and the energy transfer mechanism in the complex. The potential topics include, but are not limited to, the following:

- Antenna complex assembly and disassembly

- Structure analysis using cryo-electron microscopy (Cryo-EM) or X-ray diffraction

- Antenna functional charateristics

- Energy transfer mechnisms in antenna

- Environmental adaption mechanisms of antenna

Prof. Dr. Song Qin
Prof. Dr. Fuli Zhao
Dr. Mingyuan Xie
Dr. Wenjun Li
Guest Editors

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Keywords

  • Photosynthetic antenna
  • Structure characteristics
  • Complex assembly
  • Cryo-EM
  • X-ray diffraction
  • Functional characteristics
  • Energy transfer mechanism
  • Light absorption
  • Energy conversion devices designed and manufactured

Published Papers (2 papers)

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Research

11 pages, 1844 KiB  
Article
Detail Analysis for Energy Transfer and Pigment Assembling in C−Phycocyanin through Time−Resolved Spectroscopy and AlphaFold2
by Chao Xiao, Na Guo, Zidong Liang, Fuli Zhao and Mingyuan Xie
Crystals 2022, 12(11), 1595; https://0-doi-org.brum.beds.ac.uk/10.3390/cryst12111595 - 09 Nov 2022
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Abstract
The time-resolved fluorescence spectroscopy of the C−phycocyanin (C−PC) complex from the cyanobacterium Spirulina platensis (S. platensis) hexamer with the sub-picosecond resolution was detected, and the energy transfer pathways and related transfer rates were identified through the multiexponential analysis based on Monte-Carlo [...] Read more.
The time-resolved fluorescence spectroscopy of the C−phycocyanin (C−PC) complex from the cyanobacterium Spirulina platensis (S. platensis) hexamer with the sub-picosecond resolution was detected, and the energy transfer pathways and related transfer rates were identified through the multiexponential analysis based on Monte-Carlo method. With the purpose to construct the relationship between the functions and the structure in vivo, the three−dimension (3D) protein structure was predicted via AlphaFold2, and the arrangement of chromophores treated as the energy transfer nodes were obtained. The experiment results have been matched well with the structure prediction. This work suggests a new way to investigate structure prediction in vivo and the corresponding functions. Full article
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10 pages, 3020 KiB  
Article
Time-Resolved Fluorescence Spectroscopy Study of Energy Transfer Dynamics in Phycobilisomes from Cyanobacteria Thermosynechococcus vulcanus NIES 2134 and Synechocystis sp. PCC 6803
by Mingyuan Xie, Wenjun Li, Chao Xiao, Zhanghe Zhen, Jianfei Ma, Hanzhi Lin, Song Qin and Fuli Zhao
Crystals 2021, 11(10), 1233; https://0-doi-org.brum.beds.ac.uk/10.3390/cryst11101233 - 13 Oct 2021
Cited by 4 | Viewed by 1888
Abstract
As the largest light-harvesting complex in cyanobacteria, phycobilisomes (PBSs) show high efficiency and a high rate of energy transfer, owing to an elegant antenna-like assembly. To understand the structural influence on the dynamic process of the energy transfer in PBSs, two cyanobacterium species [...] Read more.
As the largest light-harvesting complex in cyanobacteria, phycobilisomes (PBSs) show high efficiency and a high rate of energy transfer, owing to an elegant antenna-like assembly. To understand the structural influence on the dynamic process of the energy transfer in PBSs, two cyanobacterium species Thermosynechococcus vulcanus NIES 2134 (T. 2134) and Synechocystis sp. PCC 6803 (S. 6803) with different rod–core-linked assemblies were chosen for this study. The dynamic process of the energy transfer in both PBSs was investigated through time-resolved fluorescence spectroscopy (TRFS) with a time resolution of sub-picosecond. Via the fluorescence decay curves deconvolution, the pathways and related rates of the excitation energy transfer (EET) were determined. Three time components, i.e., 10, 80, and 1250 ps, were identified in the EET in the PBSs of T. 2134 and three, i.e., 9, 115, and 1680 ps, in the EET in the PBSs of S. 6803. In addition, a comparison of the dynamic process of the energy transfer between the two cyanobacteria revealed how the PBS assembly affects the energy transfer in PBSs. The findings will provide insight into future time-resolved crystallography. Full article
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