ArticleBiochemistry2012
Hydrogen-deuterium exchange mass spectrometry reveals the interaction of Fenna-Matthews-Olson protein and chlorosome CsmA protein.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 36 citations in OpenAlex.
- Conformational modulation of the farnesoid X receptor by prenylflavonoids: Insights from hydrogen deuterium exchange mass spectrometry (HDX-MS), fluorescence titration and molecular docking studies.Biochimica et biophysica acta · 2016Article
- In situ high-resolution structure of the baseplate antenna complex in Chlorobaculum tepidum.Nature communications · 2016Article
- Localizing Carbohydrate Binding Sites in Proteins Using Hydrogen/Deuterium Exchange Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016Article
- Hybrid QM/MM study of FMO complex with polarized protein-specific charge.Scientific reports · 2015Article
- Applications of hydrogen/deuterium exchange MS from 2012 to 2014.Analytical chemistry · 2015Review
- Conformational dynamics of human FXR-LBD ligand interactions studied by hydrogen/deuterium exchange mass spectrometry: insights into the antagonism of the hypolipidemic agent Z-guggulsterone.Biochimica et biophysica acta · 2014Article
- Structural analysis of the homodimeric reaction center complex from the photosynthetic green sulfur bacterium Chlorobaculum tepidum.Biochemistry · 2014Article
- A novel mechanism for regulating the activity of proliferating cell nuclear antigen by a small protein.Nucleic acids research · 2014Article
- Computational determination of the pigment binding motif in the chlorosome protein a of green sulfur bacteria.Photosynthesis research · 2013Article
- Chlorosome antenna complexes from green photosynthetic bacteria.Photosynthesis research · 2013Review
- Mass spectrometry-based methods to study protein architecture and dynamics.Protein science : a publication of the Protein Society · 2013Review
- Native mass spectrometry of photosynthetic pigment-protein complexes.FEBS letters · 2013Review
- H/D exchange centroid monitoring is insufficient to show differences in the behavior of protein states.Journal of the American Society for Mass Spectrometry · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In green-sulfur bacterial photosynthesis, excitation energy absorbed by a peripheral antenna structure known as the chlorosome is sequentially transferred through a baseplate protein to the Fenna-Matthews-Olson (FMO) antenna protein and into the reaction center, which is embedded in the cytoplasmic membrane. The molecular details of the optimized photosystem architecture required for efficient energy transfer are only partially understood. We address here the question of how the baseplate interacts with the FMO protein by applying hydrogen/deuterium exchange coupled with enzymatic digestion and mass spectrometry analysis to reveal the binding interface of the FMO antenna protein and the CsmA baseplate protein. Several regions on the FMO protein, represented by peptides consisting of 123-129, 140-149, 150-162, 191-208, and 224-232, show significant decreases of deuterium uptake after CsmA binding. The results indicate that the CsmA protein interacts with the Bchl a #1 side of the FMO protein. A global picture including peptide-level details for the architecture of the photosystem from green-sulfur bacteria can now be drawn.
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