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External loops at the ferredoxin-NADP+ reductase protein-partner binding cavity contribute to substrates allocation

Opened Access External loops at the ferredoxin-NADP+ reductase protein-partner binding cavity contribute to substrates allocation

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Autor: Sánchez Azqueta, Ana
Martínez Júlvez, Marta
Hervás Morón, Manuel
Navarro Carruesco, José Antonio
Medina, Milagros
Departamento: Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular
Fecha: 2014
Publicado en: Biochimica et Biophysica Acta - Bioenergetics, 1837, 296-305.
Tipo de documento: Artículo
Resumen: Ferredoxin-NADP+ reductase (FNR) is the structural prototype of a family of FAD-containing reductases that catalyze electron transfer between low potential proteins and NAD(P)+/H, and that display a two-domain arrangement with an open cavity at their interface. The inner part of this cavity accommodates the reacting atoms during catalysis. Loops at its edge are highly conserved among plastidic FNRs, suggesting that they might contribute to both flavin stabilization and competent disposition of substrates. Here we pay attention to two of these loops in Anabaena FNR. The first is a sheet-loop-sheet motif, loop102-114, that allocates the FAD adenosine. It was thought to determine the extended FAD conformation, and, indirectly, to modulate isoalloxazine electronic properties, partners binding, catalytic efficiency and even coenzyme specificity. The second, loop261-269, contains key residues for the allocation of partners and coenzyme, including two glutamates, Glu267 and Glu268, proposed ...
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Cita: Sánchez Azqueta, A., Martínez Júlvez, M., Hervás Morón, M., Navarro Carruesco, J.A. y Medina, M. (2014). External loops at the ferredoxin-NADP+ reductase protein-partner binding cavity contribute to substrates allocation. Biochimica et Biophysica Acta - Bioenergetics, 1837, 296-305.
Tamaño: 1.747Mb
Formato: PDF

URI: http://hdl.handle.net/11441/68398

DOI: 10.1016/j.bbabio.2013.11.016

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