scholarly journals Probing Ultrafast Dynamics of Bacterial Reaction Centers Using Two-Dimensional Electronic Spectroscopy

Author(s):  
Andrew Niedringhaus ◽  
Veronica R. Policht ◽  
Jennifer P. Ogilvie
Author(s):  
Paul S. Furcinitti ◽  
Kathleen M. Marr ◽  
Mary K. Lyon

Photosystem II (PS II) is one of two reaction centers found in the photosynthetic membranes of eukaryotic cells. PS II converts solar to chemical energy and can split water, giving off H+ and O2. Neither bacterial reaction centers nor PS I can evolve O2, making PS II unique. Oxygen evolution involves three polypeptides (17, 24 and 33 kDa) that are exposed on the inner surface of the membrane. The remainder of PS II consists of intrinsic membrane proteins with molecular masses of 47, 43, 34, 33 and 10 kDa and multiple low molecular mass polypeptides (for review, see Hansson and Wydrzynski, 1990). In order to obtain structural information regarding PS II, and particularly the oxygen evolving-polypeptides (OEPs), we have induced the complexes to form two-dimensional crystals. The crystals are formed by sequential treatment of whole membranes with low concentrations of Triton X-100. The two-dimensional crystals are tubular, with the complexes arranged in a helical manner around the tube (Fig. 1). The tubes are being characterized by gel electrophoresis and immunoblotting, using antibodies directed against the OEPs.


2019 ◽  
Vol 205 ◽  
pp. 06014
Author(s):  
Ephraim Sommer ◽  
Antonietta De Sio ◽  
Elena Mena-Osteritz ◽  
Peter Bäuerle ◽  
Christoph Lienau

Two-dimensional electronic spectroscopy with sub-10-fs time resolution reveals signatures of vibronic coupling and wavepacket motion through a conical intersection in the initial charge separation dynamics of an acceptor-donor-acceptor oligomer thin film for organic solar cells.


2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Yin Song ◽  
Riley Sechrist ◽  
Hoang H. Nguyen ◽  
William Johnson ◽  
Darius Abramavicius ◽  
...  

AbstractPhotochemical reaction centers are the engines that drive photosynthesis. The reaction center from heliobacteria (HbRC) has been proposed to most closely resemble the common ancestor of photosynthetic reaction centers, motivating a detailed understanding of its structure-function relationship. The recent elucidation of the HbRC crystal structure motivates advanced spectroscopic studies of its excitonic structure and charge separation mechanism. We perform multispectral two-dimensional electronic spectroscopy of the HbRC and corresponding numerical simulations, resolving the electronic structure and testing and refining recent excitonic models. Through extensive examination of the kinetic data by lifetime density analysis and global target analysis, we reveal that charge separation proceeds via a single pathway in which the distinct A0 chlorophyll a pigment is the primary electron acceptor. In addition, we find strong delocalization of the charge separation intermediate. Our findings have general implications for the understanding of photosynthetic charge separation mechanisms, and how they might be tuned to achieve different functional goals.


2014 ◽  
Vol 140 (8) ◽  
pp. 084701 ◽  
Author(s):  
Justin R. Caram ◽  
Haibin Zheng ◽  
Peter D. Dahlberg ◽  
Brian S. Rolczynski ◽  
Graham B. Griffin ◽  
...  

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