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http://hdl.handle.net/10261/19746
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Título: | The atypical iron-coordination geometry of cytochrome f remains unchanged upon binding to plastocyanin, as inferred by XAS |
Autor: | Díaz-Moreno, Irene ![]() ![]() |
Palabras clave: | Cytochrome f Electron transfer Metalloproteins Plastocyanin Transient complexes X-ray absorption spectroscopy |
Fecha de publicación: | oct-2006 |
Editor: | Springer |
Citación: | Photosynthesis Research 90(1): 23-28 (2006) |
Resumen: | 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. |
Descripción: | 6 pages, 1 table, 3 figures. PMC1769345 |
Versión del editor: | http://dx.doi.org/10.1007/s11120-006-9102-8 |
URI: | http://hdl.handle.net/10261/19746 |
DOI: | 10.1007/s11120-006-9102-8 |
ISSN: | 0166-8595 (Print) 1573-5079 (Online) |
Aparece en las colecciones: | (ICMA) Artículos (IBVF) Artículos |
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