scholarly journals Porous silicon pillar structures/photosynthetic reaction centre protein hybrid for bioelectronic applications

Author(s):  
Kata Hajdu ◽  
R. Fabiola Balderas-Valadez ◽  
Alessandro Carlino ◽  
Vivechana Agarwal ◽  
László Nagy

AbstractPhotosynthetic biomaterials have attracted considerable attention at different levels of the biological organisation, from molecules to the biosphere, due to a variety of artificial application possibilities. During photosynthesis, the first steps of the conversion of light energy into chemical energy take place in a pigment–protein complex, called reaction centre (RC). In our experiments photosynthetic reaction centre protein, purified from Rhodobacter sphaeroides R-26 purple bacteria, was bound to porous silicon pillars (PSiP) after the electropolymerisation of aniline onto the surface. This new type of biohybrid material showed remarkable photoactivity in terms of measured photocurrent under light excitation in an electrochemical cell. The photocurrent was found to increase considerably after the addition of ubiquinone (UQ-0), an e−-acceptor mediator of the RC. The photoactivity of the complex was found to decrease by the addition of terbutryn, the chemical which inhibits the e−-transport on the acceptor side of the RC. In addition to the generation of sizeable light-induced photocurrents, using the PSiP/RC photoactive hybrid nanocomposite material, the system was found to be sensitive towards RC inhibitors and herbicides. This highly ordered patterned 3D structure opens new solution for designing low-power (bio-)optoelectronic, biophotonic and biosensing devices. Graphical abstract

2016 ◽  
Vol 7 (10) ◽  
pp. 6534-6550 ◽  
Author(s):  
Sai-Ho Lee ◽  
Iain M. Blake ◽  
Allan G. Larsen ◽  
James A. McDonald ◽  
Kei Ohkubo ◽  
...  

Synthetically flexible, rigid, tetrad molecules are shown to closely mimic structural and photochemical properties of the bacterial photosynthetic reaction centre.


2005 ◽  
Vol 86 (1-2) ◽  
pp. 81-100 ◽  
Author(s):  
Ashley J. Watson ◽  
Arwel V. Hughes ◽  
Paul K. Fyfe ◽  
Marion C. Wakeham ◽  
Kate Holden-Dye ◽  
...  

2003 ◽  
Vol 119 (3) ◽  
pp. 376-383 ◽  
Author(s):  
Alexander G. Ivanov ◽  
Prafullachandra Sane ◽  
Vaughan Hurry ◽  
Marianna Król ◽  
Dimitry Sveshnikov ◽  
...  

2019 ◽  
Vol 16 (151) ◽  
pp. 20180882 ◽  
Author(s):  
Adam Kell ◽  
Anton Yu. Khmelnitskiy ◽  
Tonu Reinot ◽  
Ryszard Jankowiak

The Fenna–Matthews–Olson (FMO) light-harvesting antenna protein of green sulfur bacteria is a long-studied pigment–protein complex which funnels energy from the chlorosome to the reaction centre where photochemistry takes place. The structure of the FMO protein from Chlorobaculum tepidum is known as a homotrimeric complex containing eight bacteriochlorophyll a per monomer. Owing to this structure FMO has strong intra-monomer and weak inter-monomer electronic coupling constants. While long-lived (sub-picosecond) coherences within a monomer have been a prevalent topic of study over the past decade, various experimental evidence supports the presence of subsequent inter-monomer energy transfer on a picosecond time scale. The latter has been neglected by most authors in recent years by considering only sub-picosecond time scales or assuming that the inter-monomer coupling between low-energy states is too weak to warrant consideration of the entire trimer. However, Förster theory predicts that energy transfer of the order of picoseconds is possible even for very weak (less than 5 cm –1 ) electronic coupling between chromophores. This work reviews experimental data (with a focus on emission and hole-burned spectra) and simulations of exciton dynamics which demonstrate inter-monomer energy transfer. It is shown that the lowest energy 825 nm absorbance band cannot be properly described by a single excitonic state. The energy transfer through FMO is modelled by generalized Förster theory using a non-Markovian, reduced density matrix approach to describe the electronic structure. The disorder-averaged inter-monomer transfer time across the 825 nm band is about 27 ps. While only isolated FMO proteins are presented, the presence of inter-monomer energy transfer in the context of the overall photosystem is also briefly discussed.


2017 ◽  
Vol 229 ◽  
pp. 46-56 ◽  
Author(s):  
Emiliano Altamura ◽  
Rosa Fiorentino ◽  
Francesco Milano ◽  
Massimo Trotta ◽  
Gerardo Palazzo ◽  
...  

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