ArticleNature communications2021
Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 27 citations in OpenAlex.
- Research progress on the structure of photosynthetic reaction centers-mobile electron carrier supercomplexes.Photosynthesis research · 2026Review
- Structural insights into the photochemistry of the LH1-RC complex from the marine purple phototrophic bacterium Rhodovulum sulfidophilum.Communications biology · 2026Article
- Structural basis for aerobic anoxygenic photosynthesis in the reaction center-light-harvesting 1 (RC-LH1) supercomplex of Dinoroseobacter shibae.Communications biology · 2025Article
- Long-Distance Charge Transport between Cytochrome c and Complex III is Mediated by Protons and Reactive Oxygen Species.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Cryo-EM Analysis of a Tri-Heme Cytochrome-Associated RC-LH1 Complex from the Marine Photoheterotrophic Bacterium Dinoroseobacter Shibae.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- A Native LH1-RC-HiPIP Supercomplex from an Extremophilic Phototroph.Communications biology · 2025Article
- Cryo-EM structure of HQNO-bound alternative complex III from the anoxygenic phototrophic bacterium Chloroflexus aurantiacus.The Plant cell · 2024Article
- Roadmap of electrons from donor side to the reaction center of photosynthetic purple bacteria with mutated cytochromes.Photosynthesis research · 2024Article
- A cytochrome cPlant communications · 2024Article
- The structure and assembly of reaction centre-light-harvesting 1 complexes in photosynthetic bacteria.Bioscience reports · 2023Article
- AI-driven pan-proteome analyses reveal insights into the biohydrometallurgical properties ofFrontiers in microbiology · 2023Article
- An LH1-RC photocomplex from an extremophilic phototroph provides insight into origins of two photosynthesis proteins.Communications biology · 2022Article
- Capacity and kinetics of light-induced cytochrome oxidation in intact cells of photosynthetic bacteria.Scientific reports · 2022Article
- Revisiting the concept of peptide bond planarity in an iron-sulfur protein by neutron structure analysis.Science advances · 2022Article
- Complete genome of the thermophilic purple sulfur Bacterium Thermochromatium tepidum compared to Allochromatium vinosum and other Chromatiaceae.Photosynthesis research · 2022Article
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Photosynthetic electron transfers occur through multiple components ranging from small soluble proteins to large integral membrane protein complexes. Co-crystallization of a bacterial photosynthetic electron transfer complex that employs weak hydrophobic interactions was achieved by using high-molar-ratio mixtures of a soluble donor protein (high-potential iron-sulfur protein, HiPIP) with a membrane-embedded acceptor protein (reaction center, RC) at acidic pH. The structure of the co-complex offers a snapshot of a transient bioenergetic event and revealed a molecular basis for thermodynamically unfavorable interprotein electron tunneling. HiPIP binds to the surface of the tetraheme cytochrome subunit in the light-harvesting (LH1) complex-associated RC in close proximity to the low-potential heme-1 group. The binding interface between the two proteins is primarily formed by uncharged residues and is characterized by hydrophobic features. This co-crystal structure provides a model for the detailed study of long-range trans-protein electron tunneling pathways in biological systems.
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