Recommendations for the naming of photochemical reaction centres and light-harvesting pigment-protein complexes from purple photosynthetic bacteria

1985 ◽  
Vol 806 (2) ◽  
pp. 185-186 ◽  
Author(s):  
Richard J. Cogdell ◽  
Herbert Zuber ◽  
J.Philip Thornber ◽  
Gerhart Drews ◽  
Gabriel Gingras ◽  
...  
1983 ◽  
Vol 23 (1-4) ◽  
pp. 159-169 ◽  
Author(s):  
J. Philip Thornber ◽  
Richard J. Cogdell ◽  
Beverly K. Pierson ◽  
Richard E. B. Seftor

2010 ◽  
Vol 10 (3) ◽  
pp. 401-408 ◽  
Author(s):  
Tatas H.P. Brotosudarmo ◽  
Richard J. Cogdell

Photosynthesis provides an example of a natural process that has been optimized during evolution to harness solar energy efficiently and safely, and finally to use it to produce a carbon-based fuel. Initially, solar energy is captured by the light harvesting pigment-protein complexes. In purple bacteria these antenna complexes are constructed on a rather simple modular basis. Light absorbed by these antenna complexes is funnelled downhill to reaction centres, where light drives a trans-membrane redox reaction. The light harvesting proteins not only provide the scaffolding that correctly positions the bacteriochlorophyll a and carotenoid pigments for optimal energy transfer but also creates an environment that can modulate the wavelength at which different bacteriochlorophyll molecules absorb light thereby creating the energy funnel. How these proteins can modulate the absorption spectra of the bacteriochlorophylls will be discussed in this review.


2021 ◽  
Author(s):  
Ingrid Guarnetti Prandi ◽  
Vladislav Sláma ◽  
Cristina Pecorilla ◽  
Lorenzo Cupellini ◽  
Benedetta Mennucci

Light-harvesting complexes (LHCs) are pigment-protein complexes whose main function is to capture sunlight and transfer the energy to reaction centers of photosystems. In response to varying light conditions, LH complexes also play photoregulation and photoprotection roles. In algae and mosses, a sub-family of LHCs, Light-Harvesting complex stress related (LHCSR), is responsible for photoprotective quenching. Despite their functional and evolutionary importance, no direct structural information on LHCSRs is available that can explain their unique properties. In this work we propose a structural model of LHCSR1 from the moss P. Patens, obtained through an integrated computational strategy that combines homology modeling, molecular dynamics, and multiscale quantum chemical calculations. The model is validated by reproducing the spectral properties of LHCSR1. Our model reveals the structural specificity of LHCSR1, as compared with the CP29 LH complex, and poses the basis for understanding photoprotective quenching in mosses.


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