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Modulation of copper site properties by remote residues determines the stability of plastocyanins

DOI: 10.1016/j.febslet.2010.04.013 DOI Help

Authors: Francisco Muñoz-lópez (Instituto de Bioquímica Vegetal y Fotosíntesis) , Estrella Frutos Beltran (Instituto de Bioquímica Vegetal y Fotosíntesis de Sevilla) , Sofia Diaz-moreno (Diamond Light Source) , Irene Diaz-moreno (Instituto de Bioquímica Vegetal y Fotosíntesis de Sevilla) , Gloria Subias (Instituto de Ciencia de Materiales de Aragón) , Antonio Diaz-quintana (Instituto de Bioquímica Vegetal y Fotosíntesis de Sevilla) , Miguel A. De La Rosa (Instituto de Bioquímica Vegetal y Fotosíntesis de Sevilla)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Febs Letters , VOL 584(11) , PAGES 2346-2350

State: Published (Approved)
Published: June 2010

Abstract: The 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.

Journal Keywords: Protein Stability; Metal Site Stability; Blue Copper Protein; Plastocyanin; Protein Matrix; X-Ray Absorption Spectroscopy

Subject Areas: Biology and Bio-materials, Chemistry

Facility: ESRF

Added On: 19/04/2010 14:36

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