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| Main Authors: | , , , , , , , |
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| Format: | Artículo científico |
| Language: | en |
| Published: |
Physiologia plantarum
2025
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| Subjects: | |
| Online Access: | https://pubmed.ncbi.nlm.nih.gov/40384483/ |
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| _version_ | 1868266201735495680 |
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| author | Christianson, Bern Liu, Zekun Zhang, Yingyue Wang, Chen Gardner, Adrian M Zhang, Yu-Zhong Wang, Peng Liu, Lu-Ning |
| author_facet | Christianson, Bern Liu, Zekun Zhang, Yingyue Wang, Chen Gardner, Adrian M Zhang, Yu-Zhong Wang, Peng Liu, Lu-Ning Christianson, Bern Liu, Zekun Zhang, Yingyue Wang, Chen Gardner, Adrian M Zhang, Yu-Zhong Wang, Peng Liu, Lu-Ning |
| collection | PubMed - marine biology |
| contents | Characterization of the Structure and Function of the Photosynthetic RC-LH1 Core Supercomplex From Rhodospirillum rubrum. Christianson, Bern Liu, Zekun Zhang, Yingyue Wang, Chen Gardner, Adrian M Zhang, Yu-Zhong Wang, Peng Liu, Lu-Ning Rhodospirillum rubrum Light-Harvesting Protein Complexes Photosynthesis Electron Transport Cryoelectron Microscopy Bacterial Proteins Photosynthetic reaction center-light harvesting 1 (RC-LH1) core supercomplexes are essential for energy capture and electron transport in purple bacteria. Rhodospirillum rubrum, a model organism for bacterial photosynthesis, features an RC-LH1 architecture with a closed LH1 ring and lacks the peripheral LH2 antenna in the photosynthetic membranes. How this unique RC-LH1 supercomplex performs energy transfer and quinone transport remains unclear. Here, we characterized both the structural and functional properties of Rsp. rubrum RC-LH1 supercomplex using cryo-electron microscopy (cryo-EM), transient absorption (TA) spectroscopy, and cytochrome c oxidation assays. Cryo-EM of the RC-LH1 monomeric structure revealed a closed LH1 ring of 16 αβ-polypeptides encircling the RC, with weaker RC-LH1 interactions than other RC-LH1 structures reported. TA spectra and cytochrome c oxidation assays showed that Rsp. rubrum RC-LH1 monomer with a closed LH1 ring exhibits slower and more distributed excitation energy transfer (EET) kinetics from LH1 to RC and slower electron transport rates than Rba. sphaeroides RC-LH1 monomer with a large opening in the LH1 ring. Our findings provide insight into the unique architecture and spectroscopic properties of Rsp. rubrum RC-LH1 supercomplex. This study enhances our understanding of bacterial photosynthetic mechanisms and lays the foundation for bioengineering applications in artificial photosynthetic systems. |
| format | Artículo científico |
| id | pubmed_40384483 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Physiologia plantarum |
| record_format | pubmed |
| spellingShingle | Characterization of the Structure and Function of the Photosynthetic RC-LH1 Core Supercomplex From Rhodospirillum rubrum. Christianson, Bern Liu, Zekun Zhang, Yingyue Wang, Chen Gardner, Adrian M Zhang, Yu-Zhong Wang, Peng Liu, Lu-Ning Rhodospirillum rubrum Light-Harvesting Protein Complexes Photosynthesis Electron Transport Cryoelectron Microscopy Bacterial Proteins Characterization of the Structure and Function of the Photosynthetic RC-LH1 Core Supercomplex From Rhodospirillum rubrum. Christianson, Bern Liu, Zekun Zhang, Yingyue Wang, Chen Gardner, Adrian M Zhang, Yu-Zhong Wang, Peng Liu, Lu-Ning Rhodospirillum rubrum Light-Harvesting Protein Complexes Photosynthesis Electron Transport Cryoelectron Microscopy Bacterial Proteins Photosynthetic reaction center-light harvesting 1 (RC-LH1) core supercomplexes are essential for energy capture and electron transport in purple bacteria. Rhodospirillum rubrum, a model organism for bacterial photosynthesis, features an RC-LH1 architecture with a closed LH1 ring and lacks the peripheral LH2 antenna in the photosynthetic membranes. How this unique RC-LH1 supercomplex performs energy transfer and quinone transport remains unclear. Here, we characterized both the structural and functional properties of Rsp. rubrum RC-LH1 supercomplex using cryo-electron microscopy (cryo-EM), transient absorption (TA) spectroscopy, and cytochrome c oxidation assays. Cryo-EM of the RC-LH1 monomeric structure revealed a closed LH1 ring of 16 αβ-polypeptides encircling the RC, with weaker RC-LH1 interactions than other RC-LH1 structures reported. TA spectra and cytochrome c oxidation assays showed that Rsp. rubrum RC-LH1 monomer with a closed LH1 ring exhibits slower and more distributed excitation energy transfer (EET) kinetics from LH1 to RC and slower electron transport rates than Rba. sphaeroides RC-LH1 monomer with a large opening in the LH1 ring. Our findings provide insight into the unique architecture and spectroscopic properties of Rsp. rubrum RC-LH1 supercomplex. This study enhances our understanding of bacterial photosynthetic mechanisms and lays the foundation for bioengineering applications in artificial photosynthetic systems. |
| title | Characterization of the Structure and Function of the Photosynthetic RC-LH1 Core Supercomplex From Rhodospirillum rubrum. |
| topic | Rhodospirillum rubrum Light-Harvesting Protein Complexes Photosynthesis Electron Transport Cryoelectron Microscopy Bacterial Proteins |
| url | https://pubmed.ncbi.nlm.nih.gov/40384483/ |