Artículo
The atypical iron-coordination geometry of cytochrome f remains unchanged upon binding to plastocyanin, as inferred by XAS
Autor/es | Díaz Moreno, Irene
Díaz Moreno, Sofía Subías Peruga, Maria Gloria Rosa Acosta, Miguel Ángel de la Díaz Quintana, Antonio Jesús |
Departamento | Universidad de Sevilla. Departamrnto de Bioquímica Vegetal y Biología Molecular |
Fecha de publicación | 2006-10 |
Fecha de depósito | 2017-08-21 |
Publicado en |
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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 ... 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. |
Identificador del proyecto | ESRF SC-1366
AP2000-2937 BMC2003-00458 MAT02-01221 PAI, CVI-0198 |
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. |
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