ArticleProceedings of the National Academy of Sciences of the United States of America2005
Study of the high-potential iron sulfur protein in Halorhodospira halophila confirms that it is distinct from cytochrome c as electron carrier.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- Structural insights into the photochemistry of the LH1-RC complex from the marine purple phototrophic bacterium Rhodovulum sulfidophilum.Communications biology · 2026Article
- 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
- Tunneling Mechanisms of Quinones in Photosynthetic Reaction Center-Light Harvesting 1 Supercomplexes.Small science · 2024Article
- Roadmap of electrons from donor side to the reaction center of photosynthetic purple bacteria with mutated cytochromes.Photosynthesis research · 2024Article
- Electrochemical and structural characterization of recombinant respiratory proteins of the acidophilic iron oxidizerFrontiers in microbiology · 2024Article
- Genomic Comparison, Phylogeny and Taxonomic Reevaluation of theMicroorganisms · 2022Article
- Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.Chemical reviews · 2014Review
- Nonredundant roles for cytochrome c2 and two high-potential iron-sulfur proteins in the photoferrotroph Rhodopseudomonas palustris TIE-1.Journal of bacteriology · 2014Article
- Complete genome sequence of Halorhodospira halophila SL1.Standards in genomic sciences · 2013Article
- Menaquinone as pool quinone in a purple bacterium.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
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5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The role of high-potential iron sulfur protein (HiPIP) in donating electrons to the photosynthetic reaction center in the halophilic gamma-proteobacterium Halorhodospira halophila was studied by EPR and time-resolved optical spectroscopy. A tight complex between HiPIP and the reaction center was observed. The EPR spectrum of HiPIP in this complex was drastically different from that of the purified protein and provides an analytical tool for the detection and characterization of the complexed form in samples ranging from whole cells to partially purified protein. The bound HiPIP was identified as iso-HiPIP II. Its Em value at pH 7 in the form bound to the reaction center was approximately 100 mV higher (+140 +/- 20 mV) than that of the purified protein. EPR on oriented samples showed HiPIP II to be bound in a well defined geometry, indicating the presence of specific protein-protein interactions at the docking site. At moderately reducing conditions, the bound HiPIP II donates electrons to the cytochrome subunit bound to the reaction center with a half-time of < or =11 micros. This donation reaction was analyzed by using Marcus's outer-sphere electron-transfer theory and compared with those observed in other HiPIP-containing purple bacteria. The results indicate substantial differences between the HiPIP- and the cytochrome c2-mediated re-reduction of the reaction center.
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