ArticlePhotosynthesis research2022
The PshX subunit of the photochemical reaction center from Heliobacterium modesticaldum acts as a low-energy antenna.
Article in Photosynthesis research, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Excitonic Structure and Primary Charge Separation in Purple Bacterial and Heliobacterial Reaction Centers.Plants (Basel, Switzerland) · 2026Review
- Steady-state P800 oxidation kinetics indicate that heliobacterial phototrophy is light-limited.Photosynthesis research · 2025Article
- Deletion ofApplied and environmental microbiology · 2025Article
- Anaerobic HgII reduction is driven by cellular HgII-thiol interactions.Access microbiology · 2025Article
- Identification and characterization of the low molecular mass ferredoxins involved in central metabolism in Heliomicrobium modesticaldum.Photosynthesis research · 2024Article
- What We Are Learning from the Diverse Structures of the Homodimeric Type I Reaction Center-Photosystems of Anoxygenic Phototropic Bacteria.Biomolecules · 2024Review
- Deletion of the cytochrome bc complex from Heliobacterium modesticaldum results in viable but non-phototrophic cells.Photosynthesis research · 2021Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
The anoxygenic phototrophic bacterium Heliobacterium modesticaldum contains a photochemical reaction center protein complex (called the HbRC) consisting of a homodimer of the PshA polypeptide and two copies of a newly discovered polypeptide called PshX, which is a single transmembrane helix that binds two bacteriochlorophyll g molecules. To assess the function of PshX, we produced a ∆pshX strain of Hbt. modesticaldum by leveraging the endogenous Hbt. modesticaldum Type I-A CRISPR-Cas system to aid in mutant selection. We optimized this system by separating the homologous recombination and CRISPR-based selection steps into two plasmid transformations, allowing for markerless gene replacement. Fluorescence and low-temperature absorbance of the purified HbRC from the wild-type and ∆pshX strains showed that the bacteriochlorophylls bound by PshX have the lowest site energies in the entire HbRC. This indicates that PshX acts as a low-energy antenna subunit, participating in entropy-assisted uphill energy transfer toward the P
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