We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Cryo-EM structure of a functional monomeric Photosystem I from Thermosynechococcus elongatus reveals red chlorophyll cluster.
- Authors
Çoruh, Orkun; Frank, Anna; Tanaka, Hideaki; Kawamoto, Akihiro; El-Mohsnawy, Eithar; Kato, Takayuki; Namba, Keiichi; Gerle, Christoph; Nowaczyk, Marc M.; Kurisu, Genji
- Abstract
A high-resolution structure of trimeric cyanobacterial Photosystem I (PSI) from Thermosynechococcus elongatus was reported as the first atomic model of PSI almost 20 years ago. However, the monomeric PSI structure has not yet been reported despite long-standing interest in its structure and extensive spectroscopic characterization of the loss of red chlorophylls upon monomerization. Here, we describe the structure of monomeric PSI from Thermosynechococcus elongatus BP-1. Comparison with the trimer structure gave detailed insights into monomerization-induced changes in both the central trimerization domain and the peripheral regions of the complex. Monomerization-induced loss of red chlorophylls is assigned to a cluster of chlorophylls adjacent to PsaX. Based on our findings, we propose a role of PsaX in the stabilization of red chlorophylls and that lipids of the surrounding membrane present a major source of thermal energy for uphill excitation energy transfer from red chlorophylls to P700. Çoruh, Frank et al. report the structure of monomeric Photosystem I from cyanobacteria Thermosynechoccocus elongatus BP-1. They assign monomerization-induced loss of red chlorophylls to a cluster of chlorophylls adjacent to PsaX. This study suggests a role of PsaX in the stabilization of red chlorophylls.
- Subjects
THERMOSYNECHOCOCCUS elongatus; PHOTOSYSTEMS; CHLOROPHYLL; CRYOELECTRONICS; SPECTRUM analysis
- Publication
Communications Biology, 2021, Vol 4, Issue 1, p1
- ISSN
2399-3642
- Publication type
Article
- DOI
10.1038/s42003-021-01808-9