Excitation Energy Transfer In The Light-Harvesting Antenna Of Photosynthetic Purple Bacteria: The Role Of The Long-Wavelength Absorbing Pigment B896

Author(s):  
R. van Grondelle ◽  
H. Bergstrom ◽  
V. Sundstrom ◽  
R.J. van Dorssen ◽  
M. Vos ◽  
...  
2020 ◽  
Vol 221 ◽  
pp. 59-76 ◽  
Author(s):  
Sue Ann Oh ◽  
David F. Coker ◽  
David A. W. Hutchinson

We review our recent work showing how important the site-to-site variation in coupling between chloroplasts in FMO and their protein scaffold environment is for energy transport in FMO and investigate the role of vibronic modes in this transport.


2001 ◽  
Vol 15 (28n30) ◽  
pp. 3637-3640
Author(s):  
KOICHIRO MUKAI ◽  
SHUJI ABE ◽  
HITOSHI SUMI

The rate of excitation-energy transfer (EET) within the light-harvesting complex (LH) and from LH to the reaction center (RC) of photosynthetic purple bacteria is calculated, based on a formula for EET between molecular aggregates. We show that optically forbidden exciton states participate in EET processes through mulitpole EET interactions with the help of disorder. In the antenna systems of photosynthesis, high efficiency of energy transfer is implemented by these EET processes involving optically forbidden exciton states.


2017 ◽  
Vol 14 (127) ◽  
pp. 20160896 ◽  
Author(s):  
Joshua A. Mancini ◽  
Goutham Kodali ◽  
Jianbing Jiang ◽  
Kanumuri Ramesh Reddy ◽  
Jonathan S. Lindsey ◽  
...  

Synthetic proteins designed and constructed from first principles with minimal reference to the sequence of any natural protein have proven robust and extraordinarily adaptable for engineering a range of functions. Here for the first time we describe the expression and genetic fusion of a natural photosynthetic light-harvesting subunit with a synthetic protein designed for light energy capture and multi-step transfer. We demonstrate excitation energy transfer from the bilin of the CpcA subunit (phycocyanin α subunit) of the cyanobacterial photosynthetic light-harvesting phycobilisome to synthetic four-helix-bundle proteins accommodating sites that specifically bind a variety of selected photoactive tetrapyrroles positioned to enhance energy transfer by relay. The examination of combinations of different bilin, chlorin and bacteriochlorin cofactors has led to identification of the preconditions for directing energy from the bilin light-harvesting antenna into synthetic protein–cofactor constructs that can be customized for light-activated chemistry in the cell.


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