Cryo-EM Analysis of a Tri-Heme Cytochrome-Associated RC-LH1 Complex from the Marine Photoheterotrophic Bacterium Dinoroseobacter Shibae

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F25%3A00619773" target="_blank" >RIV/61388971:_____/25:00619773 - isvavai.cz</a>
Result on the web
<a href="https://advanced.onlinelibrary.wiley.com/doi/10.1002/advs.202413456" target="_blank" >https://advanced.onlinelibrary.wiley.com/doi/10.1002/advs.202413456</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/advs.202413456" target="_blank" >10.1002/advs.202413456</a>

Result language
angličtina
Original language name
Cryo-EM Analysis of a Tri-Heme Cytochrome-Associated RC-LH1 Complex from the Marine Photoheterotrophic Bacterium Dinoroseobacter Shibae
Original language description
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 c(2) is predicted to bind at the junction between the Cyt subunit and the membrane plane, enabling electron transfer from Cyt c(2) 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.
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10606 - Microbiology

Project
<a href="/en/project/EH22_008%2F0004624" target="_blank" >EH22_008/0004624: PHOTOMACHINES - Photosynthetic cell redesign for high yields of therapeutic peptides</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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