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The atypical iron-coordination geometry of cytochrome f remains unchanged upon binding to plastocyanin, as inferred by XAS

DOI: 10.1007/s11120-006-9102-8 DOI Help
PMID: 17111237 PMID Help

Authors: Irene Díaz-moreno (Universidad de Sevilla, Spain) , Sofia Diaz-moreno (Diamond Light Source) , Gloria Subias (Universidad de Zaragoza, Spain) , Miguel A. De La Rosa (Universidad de Sevilla, Spain) , Antonio Díaz-quintana (Universidad de Sevilla, Spain)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Photosynthesis Research , VOL 90 (1) , PAGES 23 - 28

State: Published (Approved)
Published: January 2007

Open Access Open Access

Abstract: The transient complex between cytochrome f and plastocyanin from the cyanobacterium Nostoc sp. PCC 7119 has been analysed by X-ray Absorption Spectroscopy in solution, using both proteins in their oxidized and reduced states. Fe K-edge data mainly shows that the atypical metal coordination geometry of cytochrome f, in which the N-terminal amino acid acts as an axial ligand of the heme group, remains unaltered upon binding to its redox partner, plastocyanin. This fact suggests that cytochrome f provides a stable binding site for plastocyanin and minimizes the reorganization energy required in the transient complex formation, which could facilitate the electron transfer between the two redox partners.

Journal Keywords: Cytochrome f; Electron transfer; Metalloproteins; Plastocyanin; Transient complexes; X-ray absorption spectroscopy

Subject Areas: Technique Development

Facility: ESRF