Muñoz López, Francisco JesúsFrutos Beltrán, EstrellaDíaz Moreno, SofíaDíaz Moreno, IreneSubías Peruga, Maria GloriaRosa Acosta, Miguel Ángel de laDíaz Quintana, Antonio Jesús2019-03-272019-03-272010Muñoz López, F.J., Frutos Beltrán, E., Díaz Moreno, S., Díaz Moreno, I., Subías Peruga, M.G., Rosa Acosta, M.Á.d.l. y Díaz Quintana, A.J. (2010). Modulation of copper site properties by remote residues determines the stability of plastocyanins. FEBS Letters, 584 (11), 2346-2350.0014-5793 (impreso)1873-3468 (electrónico)https://hdl.handle.net/11441/84780The metal cofactor determines the thermal stability in cupredoxins, but how the redox state of copper modulates their melting points remains unknown. The metal coordination environment is highly conserved in cyanobacterial plastocyanins. However, the oxidised form is more stable than the reduced one in thermophilic Phormidium, but the opposite occurs in mesophilic Synechocystis. We have performed neutral amino‐acid substitutions at loops of Phormidium plastocyanin far from the copper site. Notably, mutation P49G/G50P confers a redox‐dependent thermal stability similar to that of the mesophilic plastocyanin. Moreover, X‐ray absorption spectroscopy reveals that P49G/G50P mutation makes the electron density distribution at the oxidised copper site shift towards that of Synechocystis plastocyanin.application/pdfengAttribution-NonCommercial-NoDerivatives 4.0 Internacionalhttp://creativecommons.org/licenses/by-nc-nd/4.0/Protein stabilityMetal site stabilityBlue copper proteinPlastocyaninProtein matrixX-ray absorption spectroscopyinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccesshttps://doi.org/10.1016/j.febslet.2010.04.013