ArticlePhotosynthesis research2012
Purification of the photosynthetic reaction center from Heliobacterium modesticaldum.
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 18 papers.
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Who cites it
18 citing papers in PubMed, 45 citations in OpenAlex.
- Excitonic Structure and Primary Charge Separation in Purple Bacterial and Heliobacterial Reaction Centers.Plants (Basel, Switzerland) · 2026Review
- Deletion ofApplied and environmental microbiology · 2025Article
- What We Are Learning from the Diverse Structures of the Homodimeric Type I Reaction Center-Photosystems of Anoxygenic Phototropic Bacteria.Biomolecules · 2024Review
- Electronic Structures of Radical-Pair-Forming Cofactors in a Heliobacterial Reaction Center.Molecules (Basel, Switzerland) · 2024Article
- The PshX subunit of the photochemical reaction center from Heliobacterium modesticaldum acts as a low-energy antenna.Photosynthesis research · 2022Article
- Deletion of the cytochrome bc complex from Heliobacterium modesticaldum results in viable but non-phototrophic cells.Photosynthesis research · 2021Article
- Reconstitution of the heliobacterial photochemical reaction center and cytochrome cPhotosynthesis research · 2020Article
- Using the Endogenous CRISPR-Cas System ofApplied and environmental microbiology · 2019Article
- Expression and purification of affinity-tagged variants of the photochemical reaction center from Heliobacterium modesticaldum.Photosynthesis research · 2019Article
- Light-driven quinone reduction in heliobacterial membranes.Photosynthesis research · 2018Article
- Evolution of photosynthetic reaction centers: insights from the structure of the heliobacterial reaction center.Photosynthesis research · 2018Article
- Emergence of cytochrome bc complexes in the context of photosynthesis.Physiologia plantarum · 2017Article
- Purification and biochemical characterization of the ATP synthase from Heliobacterium modesticaldum.Protein expression and purification · 2015Article
- Structural analysis of diheme cytochrome c by hydrogen-deuterium exchange mass spectrometry and homology modeling.Biochemistry · 2014Article
- Expression and characterization of cytochrome c553 from Heliobacterium modesticaldum.Photosynthesis research · 2014Article
- Modulation of the fluorescence yield in heliobacterial cells by induction of charge recombination in the photosynthetic reaction center.Photosynthesis research · 2014Article
- Temporal and spectral characterization of the photosynthetic reaction center from Heliobacterium modesticaldum.Photosynthesis research · 2013Article
- Chlorophyll biosynthesis gene evolution indicates photosystem gene duplication, not photosystem merger, at the origin of oxygenic photosynthesis.Genome biology and evolution · 2013Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have developed a purification protocol for photoactive reaction centers (HbRC) from Heliobacterium modesticaldum. HbRCs were purified from solubilized membranes in two sequential chromatographic steps, resulting in the isolation of a fraction containing a single polypeptide, which was identified as PshA by LC-MS/MS of tryptic peptides. All polypeptides reported earlier as unknown proteins (in Heinnickel et al., Biochemistry 45:6756-6764, 2006; Romberger et al., Photosynth Res 104:293-303, 2010) are now identified by mass spectrometry to be the membrane-bound cytochrome c (553) and four different ABC-type transporters. The purified PshA homodimer binds the following pigments: 20 bacteriochlorophyll (BChl) g, two BChl g', two 8(1)-OH-Chl a (F), and one 4,4'-diaponeurosporene. It lacks the PshB polypeptide binding the F(A) and F(B) [4Fe-4S] clusters. It is active in charge separation and exhibits a trapping time of 23 ps, as judged by time-resolved fluorescence studies. The charge recombination rate of the P(800) (+)F(X)(-) state is 10-15 ms, as seen before. The purified HbRC core was able to reduce cyanobacterial flavodoxin in the light, exhibiting a K (M) of 10 μM and a k (cat) of 9.5 s(-1) under near-saturating light. There are ~1.6 menaquinones per HbRC in the purified complex. Illumination of frozen HbRC in the presence of dithionite can cause creation of a radical at g = 2.0046, but this is not a semiquinone. Furthermore, we show that high-purity HbRCs are very stable in anoxic conditions and even remain active in the presence of oxygen under low light.
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