IBR   13079
INSTITUTO DE BIOLOGIA MOLECULAR Y CELULAR DE ROSARIO
Unidad Ejecutora - UE
capítulos de libros
Título:
Ferredoxin-NADP+ Reductases.
Autor/es:
CATALANO DUPUY, DANIELA L; RIAL, DANIELA V; CECCARELLI, EDUARDO A
Libro:
Handbook of Flavoproteins. Oxidases, Dehydrogenases and Related Systems
Editorial:
Eds. Russ Hille, Susan Miller, Bruce Palfey. Walter de Gruyter GmbH.
Referencias:
Lugar: Berlín; Año: 2012; p. 313 - 335
Resumen:
Ferredoxin-NADP+ reductases (FNRs) comprise a widespread family of hydrophilic proteins that contain firmly non-covalently bound FAD as prosthetic group. These flavoenzymes catalyze a broad range of redox reactions and participate in key metabolic pathways. In chloroplasts, FNRs take part in the last step of the photosynthetic electron transfer process, shuttling electrons from reduced ferredoxin to NADP+ in order to generate the NADPH required for CO2 assimilation. FNRs also participate in other processes such as isoprenoid biosynthesis, steroid metabolism, nitrogen fixation, xenobiotic detoxification, iron-sulfur cluster biogenesis and oxidative-stress response. This chapter focuses on the extensively-studied subfamily of plant-type FNRs found in plants, some bacteria and apicomplexan parasites. We offer a detailed description of FNR structural features, the differences encountered within the subfamily and a comprehensive outlook of the way in which the natural substrates (NADP+ and ferredoxin) interact with FNR. In this regard, we emphasize the mode in which NADP+ may enter the active site and adopt a productive conformation for catalysis. In this chapter, we compile relevant information for proper expression and purification of FNRs and discuss the spectroscopic techniques most commonly used for the analysis of these flavoproteins. Finally, we highlight significant aspects of plant-type FNRs that position them as appealing targets for biotechnological applications in the future.