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.