Photoconverters with organic semiconductors and photosynthetic bacteria: positioning the bacterial Reaction Center in nanostructures

2016 ◽  
Author(s):  
Gianluca M. Farinola ◽  
Roberta Ragni ◽  
Francesco Milano ◽  
Simona La Gatta ◽  
Roberto R. Tangorra ◽  
...  
Keyword(s):  
Reaction Center ◽  
Organic Semiconductors ◽  
Photosynthetic Bacteria ◽  
Bacterial Reaction Center

scholarly journals Polydopamine/Ethylenediamine Nanoparticles Embedding a Photosynthetic Bacterial Reaction Center for Efficient Photocurrent Generation

2021 ◽  
pp. 2000303
Author(s):  
Gabriella Buscemi ◽  
Danilo Vona ◽  
Roberta Ragni ◽  
Roberto Comparelli ◽  
Massimo Trotta ◽  
...  
Keyword(s):  
Reaction Center ◽  
Bacterial Reaction Center ◽  
Photocurrent Generation

scholarly journals Quantum coherence as a witness of vibronically hot energy transfer in bacterial reaction center

2017 ◽  
Vol 3 (9) ◽  
pp. e1603141 ◽  
Author(s):  
David Paleček ◽  
Petra Edlund ◽  
Sebastian Westenhoff ◽  
Donatas Zigmantas
Keyword(s):  
Energy Transfer ◽  
Reaction Center ◽  
Quantum Coherence ◽  
Bacterial Reaction Center

The Three-Dimensional Structure of the Herbicide Binding Niche on the Reaction Center Polypeptides of Photosystem II

1987 ◽  
Vol 42 (6) ◽  
pp. 742-750 ◽  
Author(s):  
Achim Trebst
Keyword(s):  
Amino Acid ◽  
Photosystem Ii ◽  
Reaction Center ◽  
Three Dimensional ◽  
Chemical Compounds ◽  
Dimensional Structure ◽  
Bacterial Reaction Center ◽  
Protein Subunits ◽  
Herbicide Binding ◽  
Hydropathy Analysis

The folding through the membrane of the plastoquinone and herbicide binding protein subunits of photosystem II and the topology of the binding niche for plastoquinone and herbicides is described. The model is based on the homology in amino acid sequence and folding prediction from the hydropathy analysis of the D-1 and D-2 subunits of photosystem II to the reaction center polypeptides L and M of the bacterial reaction center. It incorporates the amino acid changes in the D-1 polypeptide in herbicide tolerant plants and those indicated by chemical tagging to be involved in Qв binding. It proposes homologous amino acids in the D-1/D-2 polypeptides to those indicated by the X-ray structure of the bacterial reaction center to be involved in Fe-, quinone- and reaction center chlorophyll-binding. The different chemical compounds known to interfere with Qв function are grouped into two families depending on their orientation in the Qв binding niche.

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