IBR   13079
INSTITUTO DE BIOLOGIA MOLECULAR Y CELULAR DE ROSARIO
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Molecular insights into the electron transfer mechanism in the Rhodobacter capsulatus FPR
Autor/es:
PONCE, ALMUDENA; BORTOLOTTI, ANA; CORTEZ, NÉSTOR; HERMOSO, JUAN A.; MAYA, CELIA
Lugar:
Sevilla
Reunión:
Congreso; 22nd IUBMB and 37th FEBS; 2012
Institución organizadora:
Fed.European Biochemical Societies and IUBMB Int. Union for Biochemistry and Molecular Biology
Resumen:
Ferredoxin:NADP(H) reductases (FNRs/FPRs, EC 1.18.1.2) carry out the transference of two electrons between two molecules of a mono-electron carrier (flavodoxin or ferredoxin) and the NADP(H), by a reversible mechanism [1]. FPR from R. capsulatus is a bacterial ferredoxin:NADP(H) reductase proposed to shuttle electrons from the NADPH pool of the cell to the flavodoxin NifF, a potential electron carrier of the nitrogenase [2-3]. The FPR and NifF structures have been recently resolved and, in order to elucidate the electron transfer mechanism of this redox system, we are going to undertake the structural characterization of the several active-site mutants of the FPR enzyme by X-Ray Crystallography.Crystallization assays will be carrying out using the recombinant proteins and their structures will be solved by the Molecular Replacement Method on the basis of the native FPR structure (PDB code 2BGI). References: [1] A.K. Arakaki, E.A. Ceccarelli, N. Carrillo (1997) Plant-type ferredoxin-NADP+ reductases: a basal structural framework and a multiplicity of functions, FASEB J. 11, 133?140. [2] C. Bittel, L. C. Tabares, M. Armesto, N. Carrillo, N. Cortez (2003) The oxidant-responsive diaphorase of Rhodobacter capsulatus is a ferredoxin (flavodoxin)-NADP(H) reductase, FEBS Lett. 553, 408?412. [3] I. Nogués, I. Pérez-Dorado, S. Frago, C. Bittel, S. G. Mayhew, C. Gómez-Moreno, J. A. Hermoso, M. Medina, N. Cortez, N. Carrillo (2005) The Ferredoxin-NADP(H) Reductase from Rhodobacter capsulatus: Molecular Structure and Catalytic Mechanism, Biochemistry 44, 11730-11740.