Cryo-EM Analysis of a Tri-Heme Cytochrome-Associated RC-LH1 Complex from the Marine Photoheterotrophic Bacterium Dinoroseobacter Shibae
Language English Country Germany Media print-electronic
Document type Journal Article
Grant support
LR22C010001
Zhejiang Provincial Natural Science Foundation of China
32100202
National Natural Science Foundation of China
42188102
National Natural Science Foundation of China
42222604
National Natural Science Foundation of China
CZ.02.01.01/00/22_008/0004624
Project Photomachines, Czech Ministry of Education Youth and Sports OP JAK program
NSERC RGPIN 2018-03898
Natural Sciences and Engineering Research Council
Ministry of Science and Technology (ONCE)
PubMed
40112203
PubMed Central
PMC12079452
DOI
10.1002/advs.202413456
Knihovny.cz E-resources
- Keywords
- energy transfer, photoheterotrophic bacteria, photosynthesis, reaction center, structure,
- MeSH
- Bacterial Proteins metabolism chemistry MeSH
- Cryoelectron Microscopy methods MeSH
- Photosynthesis physiology MeSH
- Heme metabolism chemistry MeSH
- Light-Harvesting Protein Complexes * metabolism ultrastructure chemistry MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Bacterial Proteins MeSH
- Heme MeSH
- Light-Harvesting Protein Complexes * MeSH
The reaction center-light harvesting 1 (RC-LH1) complex converts solar energy into electrical energy, driving the initiation of photosynthesis. The authors present a cryo-electron microscopy structure of the RC-LH1 isolated from a marine photoheterotrophic bacterium Dinoroseobacter shibae. The RC comprises four subunits, including a three-heme cytochrome (Cyt) c protein, and is surrounded by a closed LH ring composed of 17 pairs of antenna subunits. Notably, a novel subunit with an N-terminal "helix-turn-helix" motif embedded in the gap between the RC and the LH ring is identified. The purified RC-LH1 complex exhibits high stability in solutions containing Mg2+ or Ca2+. The periplasmic Cyt c2 is predicted to bind at the junction between the Cyt subunit and the membrane plane, enabling electron transfer from Cyt c2 to the proximal heme of the tri-heme Cyt, and subsequently to the special pair of bacteriochlorophylls. These findings provide structural insights into the efficient energy and electron transfer processes within a distinct type of RC-LH1, and shed light on evolutionary adaptations of photosynthesis.
College of Life Sciences Zhejiang University Hangzhou Zhejiang 310058 China
Department of Microbiology and Immunology University of British Columbia Vancouver BC V6T 1Z3 Canada
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