ArticlePhotosynthesis research
Importance of a single disulfide bond for the PsbO protein of photosystem II: protein structure stability and soluble overexpression in Escherichia coli.
Article in Photosynthesis research. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Some useful ideas for multistate protein design: Effect of amino acid substitutions on the multistate proteins stability and the rate of protein structure formation.Frontiers in molecular biosciences · 2022Article
- Current Knowledge on Mechanisms Preventing Photosynthesis Redox Imbalance in Plants.Antioxidants (Basel, Switzerland) · 2021Review
- NbPsbO1 Interacts Specifically with theJournal of virology · 2021Article
- Intrinsic Disorder-Based Design of Stable Globular Proteins.Biomolecules · 2019Article
- Protein crystallization and initial neutron diffraction studies of the photosystem II subunit PsbO.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Operation of trans-thylakoid thiol-metabolizing pathways in photosynthesis.Frontiers in plant science · 2013Article
- Functional recombinant extra membrane loop of human CD20, an alternative of the full length CD20 antigen.Iranian biomedical journal · 2012Article
- Article
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Authors and funding
8 authors.
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Abstract
PsbO protein is an important constituent of the water-oxidizing complex, located on the lumenal side of photosystem II. We report here the efficient expression of the spinach PsbO in E. coli where the solubility depends entirely on the formation of the disulfide bond. The PsbO protein purified from a pET32 system that includes thioredoxin fusion is properly folded and functionally active. Urea unfolding experiments imply that the reduction of the single disulfide bridge decreases stability of the protein. Analysis of inter-residue contact density through the PsbO molecule shows that Cys51 is located in a cluster with high contact density. Reduction of the Cys28-Cys51 bond is proposed to perturb the packing interactions in this cluster and destabilize the protein as a whole. Taken together, our results give evidence that PsbO exists in solution as a compact highly ordered structure, provided that the disulfide bridge is not reduced.
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