ArticlePhotosynthesis research2012
The FX iron-sulfur cluster serves as the terminal bound electron acceptor in heliobacterial reaction centers.
Article in Photosynthesis research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 24 citations in OpenAlex.
- Article
- Molecular design principles for Photosystem I-based biohybrid solar fuel catalysts.bioRxiv : the preprint server for biology · 2026Article
- Research progress on the structure of photosynthetic reaction centers-mobile electron carrier supercomplexes.Photosynthesis research · 2026Review
- Steady-state P800 oxidation kinetics indicate that heliobacterial phototrophy is light-limited.Photosynthesis research · 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
- Energetic Diversity in the Electron-Transfer Pathways of Type I Photosynthetic Reaction Centers.Biochemistry · 2023Article
- Shedding Light on Primary Donors in Photosynthetic Reaction Centers.Frontiers in microbiology · 2021Review
- Evolution of photosynthetic reaction centers: insights from the structure of the heliobacterial reaction center.Photosynthesis research · 2018Article
- Light-driven quinone reduction in heliobacterial membranes.Photosynthesis research · 2018Article
- Evolution of the acceptor side of photosystem I: ferredoxin, flavodoxin, and ferredoxin-NADPPhotosynthesis research · 2017Review
- Controlling electron transfer between the two cofactor chains of photosystem I by the redox state of one of their components.Biophysical journal · 2015Article
- Modulation of the fluorescence yield in heliobacterial cells by induction of charge recombination in the photosynthetic reaction center.Photosynthesis research · 2014Article
- Purification of the photosynthetic reaction center from Heliobacterium modesticaldum.Photosynthesis research · 2012Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Phototrophs of the family Heliobacteriaceae contain the simplest known Type I reaction center (RC), consisting of a homodimeric (PshA)(2) core devoid of bound cytochromes and antenna proteins. Unlike plant and cyanobacterial Photosystem I in which the F(A)/F(B) protein, PsaC, is tightly bound to P(700)-F(X) cores, the RCs of Heliobacterium modesticaldum contain two F(A)/F(B) proteins, PshBI and PshBII, which are loosely bound to P(800)-F(X) cores. These two 2[4Fe-4S] ferredoxins have been proposed to function as mobile redox proteins, reducing downstream metabolic partners much in the same manner as does [2Fe-2S] ferredoxin or flavodoxin (Fld) in PS I. Using P(800)-F(X) cores devoid of PshBI and PshBII, we show that iron-sulfur cluster F(X) directly reduces Fld without the involvement of F(A) or F(B) (Fld is used as a proxy for soluble redox proteins even though a gene encoding Fld is not identified in the H. modesticaldum genome). The reduction of Fld is suppressed by the addition of PshBI or PshBII, an effect explained by competition for the electron on F(X). In contrast, P(700)-F(X) cores require the presence of the PsaC, and hence, the F(A)/F(B) clusters for Fld (or ferredoxin) reduction. Thus, in H. modesticaldum, the interpolypeptide F(X) cluster serves as the terminal bound electron acceptor. This finding implies that the homodimeric (PshA)(2) cores should be capable of donating electrons to a wide variety of yet-to-be characterized soluble redox partners.
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