CONFIGURATIONS OF CAROTENOIDS IN THE REACTION CENTER and THE LIGHT-HARVESTING COMPLEX OF Rhodospirillum rubrum. NATURAL SELECTION OF CAROTENOID CONFIGURATIONS BY PIGMENT PROTEIN COMPLEXES

1990 ◽  
Vol 51 (1) ◽  
pp. 119-128 ◽  
Author(s):  
Yasushi Koyama ◽  
Ichiro Takatsuka ◽  
Mariko Kanaji ◽  
Koichi Tomimoto ◽  
Mariko Kito ◽  
...  
Keyword(s):  
Natural Selection ◽  
Reaction Center ◽  
Rhodospirillum Rubrum ◽  
Light Harvesting ◽  
Protein Complexes ◽  
Light Harvesting Complex ◽  
Pigment Protein Complexes ◽  
Selection Of

scholarly journals Structure of the stress-related LHCSR1 complex determined by an integrated computational strategy

2021 ◽  
Author(s):  
Ingrid Guarnetti Prandi ◽  
Vladislav Sláma ◽  
Cristina Pecorilla ◽  
Lorenzo Cupellini ◽  
Benedetta Mennucci
Keyword(s):  
Structural Model ◽  
Light Harvesting ◽  
Structural Information ◽  
Protein Complexes ◽  
Complex Stress ◽  
Main Function ◽  
Light Harvesting Complexes ◽  
Light Harvesting Complex ◽  
Pigment Protein Complexes ◽  
Computational Strategy

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.

Research on Entanglement and Coherence in Light Harvesting Complex during Photosynthesis

2013 ◽  
Vol 641-642 ◽  
pp. 927-930
Author(s):  
Xing Yu Guan ◽  
J. Chee
Keyword(s):  
Energy Transport ◽  
Light Harvesting ◽  
Protein Complexes ◽  
Green Plant ◽  
Light Harvesting Complex ◽  
Transport Efficiency ◽  
The Past ◽  
Pigment Protein Complexes

Photosynthesis is a wonderful phenomenon which is present in green plant. In recent years, it has been discovered that there is entanglement in the biological pigment protein complexes, and that may be the reason of high transport efficiency. And coherence also plays an important role during the process of this efficiency energy transport. However, some scientists consider that it is not at all clear entanglement exists in the FMO complex, or unlike coherence, its role for the transport efficiency seems to be irrelevant. This paper mainly introduces what progress have scientists made during the past few years.

scholarly journals Role of the H Protein in Assembly of the Photochemical Reaction Center and Intracytoplasmic Membrane inRhodospirillum rubrum

2000 ◽  
Vol 182 (5) ◽  
pp. 1200-1207 ◽  
Author(s):  
Yongjian S. Cheng ◽  
Christine A. Brantner ◽  
Alexandre Tsapin ◽  
Mary Lynne Perille Collins
Keyword(s):  
Reaction Center ◽  
Photochemical Reaction ◽  
Rhodospirillum Rubrum ◽  
Protein Complexes ◽  
Open Reading Frames ◽  
Intracytoplasmic Membrane ◽  
Membrane Formation ◽  
Pigment Protein Complexes ◽  
Light Harvesting Antenna ◽  
Phototrophic Growth

ABSTRACT Rhodospirillum rubrum is a model for the study of membrane formation. Under conditions of oxygen limitation, this facultatively phototrophic bacterium forms an intracytoplasmic membrane that houses the photochemical apparatus. This apparatus consists of two pigment-protein complexes, the light-harvesting antenna (LH) and photochemical reaction center (RC). The proteins of the photochemical components are encoded by the puf operon (LHα, LHβ, RC-L, and RC-M) and by puhA (RC-H). R. rubrum puf interposon mutants do not form intracytoplasmic membranes and are phototrophically incompetent. The puh region was cloned, and DNA sequence determination identified open reading framesbchL and bchM and part of bchH;bchHLM encode enzymes of bacteriochlorophyll biosynthesis. A puhA/G115 interposon mutant was constructed and found to be incapable of phototrophic growth and impaired in intracytoplasmic membrane formation. Comparison of properties of the wild-type and the mutated and complemented strains suggests a model for membrane protein assembly. This model proposes that RC-H is required as a foundation protein for assembly of the RC and highly developed intracytoplasmic membrane. In complemented strains, expression of puhoccurred under semiaerobic conditions, thus providing the basis for the development of an expression vector. The puhA gene alone was sufficient to restore phototrophic growth provided that recombination occurred.

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