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Título

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

AutorDíaz-Moreno, Irene ; Díaz-Moreno, Sofía; Subías, G.; Rosa, Miguel A. de la ; Díaz-Quintana, Antonio
Palabras claveCytochrome f
Electron transfer
Metalloproteins
Plastocyanin
Transient complexes
X-ray absorption spectroscopy
Fecha de publicaciónoct-2006
EditorSpringer
CitaciónPhotosynthesis Research 90(1): 23-28 (2006)
ResumenThe 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.
Descripción6 pages, 1 table, 3 figures.
PMC1769345
Versión del editorhttp://dx.doi.org/10.1007/s11120-006-9102-8
URIhttp://hdl.handle.net/10261/19746
DOI10.1007/s11120-006-9102-8
ISSN0166-8595 (Print)
1573-5079 (Online)
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