Molecular asymmetry of a photosynthetic supercomplex from green sulfur bacteria

Ryan Puskar, Chloe Truong, Kyle Swain, Saborni Chowdhury, Ka-Yi Chan, Shan Li, Kai-Wen Cheng, Ting Yu Wang, Yu-Ping Poh, Yuval Mazor, Haijun Liu, Tsui-Fen Chou, Brent L. Nannenga and Po-Lin Chiu ()
Additional contact information
Ryan Puskar: Arizona State University
Chloe Truong: Arizona State University
Kyle Swain: Arizona State University
Saborni Chowdhury: Arizona State University
Ka-Yi Chan: Arizona State University
Shan Li: California Institute of Technology
Kai-Wen Cheng: California Institute of Technology
Ting Yu Wang: California Institute of Technology
Yu-Ping Poh: Arizona State University
Yuval Mazor: Arizona State University
Haijun Liu: Washington University
Tsui-Fen Chou: California Institute of Technology
Brent L. Nannenga: Arizona State University
Po-Lin Chiu: Arizona State University

Nature Communications, 2022, vol. 13, issue 1, 1-12

Abstract: Abstract The photochemical reaction center (RC) features a dimeric architecture for charge separation across the membrane. In green sulfur bacteria (GSB), the trimeric Fenna-Matthews-Olson (FMO) complex mediates the transfer of light energy from the chlorosome antenna complex to the RC. Here we determine the structure of the photosynthetic supercomplex from the GSB Chlorobaculum tepidum using single-particle cryogenic electron microscopy (cryo-EM) and identify the cytochrome c subunit (PscC), two accessory protein subunits (PscE and PscF), a second FMO trimeric complex, and a linker pigment between FMO and the RC core. The protein subunits that are assembled with the symmetric RC core generate an asymmetric photosynthetic supercomplex. One linker bacteriochlorophyll (BChl) is located in one of the two FMO-PscA interfaces, leading to differential efficiencies of the two energy transfer branches. The two FMO trimeric complexes establish two different binding interfaces with the RC cytoplasmic surface, driven by the associated accessory subunits. This structure of the GSB photosynthetic supercomplex provides mechanistic insight into the light excitation energy transfer routes and a possible evolutionary transition intermediate of the bacterial photosynthetic supercomplex from the primitive homodimeric RC.

Date: 2022
References: View references in EconPapers View complete reference list from CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/s41467-022-33505-4 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-33505-4

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-022-33505-4

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().