Transient binding of plastocyanin to its physiological redox partners modifies the copper site geometry

DOI: 10.1016/j.febslet.2006.10.020

Authors: Irene Díaz-Moreno (Universidad de Sevilla y Consejo Superior de Investigaciones Científicas) , Antonio Diaz-Quintana (Universidad de Sevilla y Consejo Superior de Investigaciones Científicas) , Sofia Diaz-Moreno (Diamond Light Source) , Gloria Subias (Universidad de Zaragoza y Consejo Superior de Investigaciones Científicas) , Miguel A. De La Rosa (Universidad de Sevilla y Consejo Superior de Investigaciones Científicas)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Febs Letters , VOL 580 (26) , PAGES 6187 - 6194

State: Published (Approved)
Published: November 2006

Abstract: The transient complexes of plastocyanin with cytochrome f and photosystem I are herein used as excellent model systems to investigate how the metal sites adapt to the changes in the protein matrix in transient complexes that are involved in redox reactions. Thus, both complexes from the cyanobacterium Nostoc sp. PCC 7119 (former Anabaena sp. PCC 7119) have been analysed by X-ray absorption spectroscopy. Our data are consistent with a significant distortion of the trigonal pyramidal geometry of the Cu coordination sphere when plastocyanin binds to cytochrome f, no matter their redox states are. The resulting tetrahedral geometry shows a shortening of the distance between Cu and the Sδ atom of its ligand Met-97, with respect to the crystallographic structure of free plastocyanin. On the other hand, when plastocyanin binds to photosystem I instead of cytochrome f, the geometric changes are not significant but a displacement in charge distribution around the metal centre can be observed. Noteworthy, the electronic density around the Cu atom increases or decreases when oxidised plastocyanin binds to cytochrome f or photosystem I, respectively, thus indicating that the protein matrix affects the electron transfer between the two partners during their transient interaction.

Journal Keywords: Electron transfer; Metalloproteins; Plastocyanin; Protein matrix; Transient complexes; X-ray absorption spectroscopy

Subject Areas: Biology and Bio-materials, Chemistry

Facility: BM29 at ESRF

Added On: 01/02/2016 14:16

Discipline Tags:

Biochemistry Chemistry Life Sciences & Biotech

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