Energy Transfer Dynamics in Light-Harvesting Complex 2 Variants Containing Oxidized B800 Bacteriochlorophyll a

2021 ◽  
Author(s):  
Yoshitaka Saga ◽  
Yuji Otsuka ◽  
Aiko Tanaka ◽  
Yuto Masaoka ◽  
Tsubasa Hidaka ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Light Harvesting ◽  
Bacteriochlorophyll A ◽  
Light Harvesting Complex

B800–B850 coherence correlates with energy transfer rates in the LH2 complex of photosynthetic purple bacteria

2015 ◽  
Vol 17 (46) ◽  
pp. 30805-30816 ◽  
Author(s):  
Cathal Smyth ◽  
Daniel G. Oblinsky ◽  
Gregory D. Scholes
Keyword(s):  
Energy Transfer ◽  
Quantum Information ◽  
Information Science ◽  
Light Harvesting ◽  
Purple Bacteria ◽  
Quantum Information Science ◽  
Light Harvesting Complex ◽  
Transfer Rates ◽  
Photosynthetic Purple Bacteria

Delocalization of a model light-harvesting complex is investigated using multipartite measures inspired by quantum information science.

Extension of Light-Harvesting Ability of Photosynthetic Light-Harvesting Complex 2 (LH2) through Ultrafast Energy Transfer from Covalently Attached Artificial Chromophores

2015 ◽  
Vol 137 (40) ◽  
pp. 13121-13129 ◽  
Author(s):  
Yusuke Yoneda ◽  
Tomoyasu Noji ◽  
Tetsuro Katayama ◽  
Naoto Mizutani ◽  
Daisuke Komori ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Light Harvesting ◽  
Light Harvesting Complex

Structure of the maize photosystem I supercomplex with light-harvesting complexes I and II

Science ◽  
2018 ◽  
Vol 360 (6393) ◽  
pp. 1109-1113 ◽  
Author(s):  
Xiaowei Pan ◽  
Jun Ma ◽  
Xiaodong Su ◽  
Peng Cao ◽  
Wenrui Chang ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Energy Transfer ◽  
Complex I ◽  
Light Harvesting ◽  
Light Conditions ◽  
Light Harvesting Complexes ◽  
Light Harvesting Complex ◽  
Cryo Electron Microscopy ◽  
Photosystems I And Ii ◽  
Light Harvesting Complex Ii

Plants regulate photosynthetic light harvesting to maintain balanced energy flux into photosystems I and II (PSI and PSII). Under light conditions favoring PSII excitation, the PSII antenna, light-harvesting complex II (LHCII), is phosphorylated and forms a supercomplex with PSI core and the PSI antenna, light-harvesting complex I (LHCI). Both LHCI and LHCII then transfer excitation energy to the PSI core. We report the structure of maize PSI-LHCI-LHCII solved by cryo–electron microscopy, revealing the recognition site between LHCII and PSI. The PSI subunits PsaN and PsaO are observed at the PSI-LHCI interface and the PSI-LHCII interface, respectively. Each subunit relays excitation to PSI core through a pair of chlorophyll molecules, thus revealing previously unseen paths for energy transfer between the antennas and the PSI core.

Plant and Algal PSII–LHCII Supercomplexes: Structure, Evolution and Energy Transfer

2021 ◽  
Author(s):  
Xin Sheng ◽  
Zhenfeng Liu ◽  
Eunchul Kim ◽  
Jun Minagawa
Keyword(s):  
Energy Transfer ◽  
Light Harvesting ◽  
Chemical Form ◽  
Structure Evolution ◽  
Light Harvesting Complex ◽  
Green Algal ◽  
Cryo Electron Microscopy ◽  
Light Harvesting Complex Ii ◽  
Overall Efficiency ◽  
Psii Subunits

Abstract Photosynthesis is the process conducted by plants and algae to capture photons and store their energy into a chemical form. The light-harvesting, excitation transfer, charge separation, and electron transfer in photosystem II (PSII) are the critical initial reactions of photosynthesis and thereby largely determine its overall efficiency. In this review, we outline the rapidly accumulating knowledges about the architectures and assemblies of plant and green algal PSII–light harvesting complex II (LHCII) supercomplexes with a particular focus on new insights provided by the recent high-resolution cryo-electron microscopy (cryo-EM) map of the supercomplexes from a green alga Chlamydomonas reinhardtii. We make pair-wise comparative analyses between the supercomplexes from plants and green algae to gain insights about the evolution of the PSII–LHCII supercomplexes involving the peripheral small PSII subunits that might have been acquired during the evolution, and about the energy transfer pathways that define their light-harvesting and photoprotective properties.

Probing the bacteriochlorophyll binding site by reconstitution of the light-harvesting complex of Rhodospirillum rubrum with bacteriochlorophyll a analogs

Biochemistry ◽  
1990 ◽  
Vol 29 (12) ◽  
pp. 2951-2960 ◽  
Author(s):  
Pamela S. Parkes-Loach ◽  
Tomasz J. Michalski ◽  
Wendy J. Bass ◽  
Ursula Smith ◽  
Paul A. Loach
Keyword(s):  
Binding Site ◽  
Rhodospirillum Rubrum ◽  
Light Harvesting ◽  
Bacteriochlorophyll A ◽  
Light Harvesting Complex
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