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Importance of a single disulfide bond for the PsbO protein of photosystem II: protein structure stability and soluble overexpression in Escherichia coli.
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Institutionen för fysiologisk botanik. Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Umeå Plant Science Centre (UPSC).
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2008 (engelsk)Inngår i: Photosynthesis Research, ISSN 0166-8595, E-ISSN 1573-5079, Vol. 98, s. 391-403Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

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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2008. Vol. 98, s. 391-403
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URN: urn:nbn:se:umu:diva-10932DOI: 10.1007/s11120-008-9327-9ISI: 000261577900034PubMedID: 18709441OAI: oai:DiVA.org:umu-10932DiVA, id: diva2:150603
Tilgjengelig fra: 2009-01-13 Laget: 2009-01-13 Sist oppdatert: 2020-02-05bibliografisk kontrollert

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