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

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

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Autor: Díaz Moreno, Irene
Díaz Moreno, Sofía
Subías Peruga, Maria Gloria
De la Rosa Acosta, Miguel Ángel
Díaz Quintana, Antonio
Departamento: Universidad de Sevilla. Departamrnto de Bioquímica Vegetal y Biología Molecular
Fecha: 2006-10
Publicado en: Photosynthesis Research, 90 (1), 23-28.
Tipo de documento: Artículo
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.
Cita: Díaz Moreno, I., Díaz Moreno, S., Subías Peruga, M.G., De la Rosa Acosta, M.Á. y Díaz Quintana, A. (2006). The atypical iron-coordination geometry of cytochrome f remains unchanged upon binding to plastocyanin, as inferred by XAS. Photosynthesis Research, 90 (1), 23-28.
Tamaño: 163.2Kb
Formato: PDF

URI: http://hdl.handle.net/11441/63899

DOI: 10.1007/s11120-006-9102-8

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