The FASEB Journal, Vol 11, 133-140, Copyright © 1997 by The Federation of American Societies for Experimental Biology

REVIEWS

Plant-type ferredoxin-NADP+ reductases: a basal structural framework and a multiplicity of functions

AK Arakaki, EA Ceccarelli and N Carrillo
Molecular Biology Division, PROMUBIE, Facultad de Ciencias Bioquimicasy Farmaceuticas, Universidad Nacional de Rosario, Argentina.

Ferredoxin-NADP+ (oxido)reductase (EC 1.18.1.2, FNR) is an FAD- containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of this flavoprotein are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. Although ferredoxin-NADP+ reductases have been thoroughly investigated and their properties reviewed on several occasions, considerable advances in the understanding of these flavoenzymes have occurred in the last few years, including the characterization of cDNA and genomic clones encoding FNR proteins from plants, algae, vertebrates, and bacteria, determination of the atomic structure of a plant FNR at high resolution, and the expression of functional reductases in microorganisms like Escherichia coli and Saccharomyces cerevisiae. The aim of this article is to summarize information gained through these recent developments, including the phylogenetic relationships among ferredoxin reductases and the key structural features of the plant FNR family. Other aspects such as the catalytic mechanism of FNR and the molecular events underlying biogenesis, intracellular sorting, folding, and holoenzyme assembly of this important flavoenzyme are also discussed in some detail. Ferredoxin-NADP+ reductases display several outstanding properties that make them excellent model proteins to address broad biological questions.

This article has been cited by other articles:

				J. O. Gummadova, G. J. Fletcher, A. Moolna, G. T. Hanke, T. Hase, and C. G. Bowsher Expression of multiple forms of ferredoxin NADP+ oxidoreductase in wheat leaves J. Exp. Bot., November 1, 2007; 58(14): 3971 - 3985. [Abstract] [Full Text] [PDF]

				Y.-H. Lee, K. Tamura, M. Maeda, M. Hoshino, K. Sakurai, S. Takahashi, T. Ikegami, T. Hase, and Y. Goto Cores and pH-dependent Dynamics of Ferredoxin-NADP+ Reductase Revealed by Hydrogen/Deuterium Exchange J. Biol. Chem., February 23, 2007; 282(8): 5959 - 5967. [Abstract] [Full Text] [PDF]

				T. Nosenko, K. L. Lidie, F. M. Van Dolah, E. Lindquist, J.-F. Cheng, US Department of Energy-Joint Genome Institute, and D. Bhattacharya Chimeric Plastid Proteome in the Florida "Red Tide" Dinoflagellate Karenia brevis Mol. Biol. Evol., November 1, 2006; 23(11): 2026 - 2038. [Abstract] [Full Text] [PDF]

				D. V. Rial, J. Ottado, and E. A. Ceccarelli Precursors with Altered Affinity for Hsp70 in Their Transit Peptides Are Efficiently Imported into Chloroplasts J. Biol. Chem., November 21, 2003; 278(47): 46473 - 46481. [Abstract] [Full Text] [PDF]

				V. Pandini, G. Caprini, N. Thomsen, A. Aliverti, F. Seeber, and G. Zanetti Ferredoxin-NADP+ Reductase and Ferredoxin of the Protozoan Parasite Toxoplasma gondii Interact Productively in Vitro and in Vivo J. Biol. Chem., December 6, 2002; 277(50): 48463 - 48471. [Abstract] [Full Text] [PDF]

				M. Maeda, D. Hamada, M. Hoshino, Y. Onda, T. Hase, and Y. Goto Partially Folded Structure of Flavin Adenine Dinucleotide-depleted Ferredoxin-NADP+ Reductase with Residual NADP+ Binding Domain J. Biol. Chem., May 3, 2002; 277(19): 17101 - 17107. [Abstract] [Full Text] [PDF]

				A. R. Krapp, R. E. Rodriguez, H. O. Poli, D. H. Paladini, J. F. Palatnik, and N. Carrillo The Flavoenzyme Ferredoxin (Flavodoxin)-NADP(H) Reductase Modulates NADP(H) Homeostasis during the soxRS Response of Escherichia coli J. Bacteriol., March 1, 2002; 184(5): 1474 - 1480. [Abstract] [Full Text] [PDF]

				L. Piubelli, A. Aliverti, A. K. Arakaki, N. Carrillo, E. A. Ceccarelli, P. A. Karplus, and G. Zanetti Competition between C-terminal Tyrosine and Nicotinamide Modulates Pyridine Nucleotide Affinity and Specificity in Plant Ferredoxin-NADP+ Reductase J. Biol. Chem., March 31, 2000; 275(14): 10472 - 10476. [Abstract] [Full Text] [PDF]

				A. Aliverti, Z. Deng, D. Ravasi, L. Piubelli, P. A. Karplus, and G. Zanetti Probing the Function of the Invariant Glutamyl Residue 312 in Spinach Ferredoxin-NADP+ Reductase J. Biol. Chem., December 18, 1998; 273(51): 34008 - 34015. [Abstract] [Full Text] [PDF]

				A. Dorowski, A. Hofmann, C. Steegborn, M. Boicu, and R. Huber Crystal Structure of Paprika Ferredoxin-NADP+ Reductase. IMPLICATIONS FOR THE ELECTRON TRANSFER PATHWAY J. Biol. Chem., March 16, 2001; 276(12): 9253 - 9263. [Abstract] [Full Text] [PDF]

				M. Medina, A. Luquita, J. Tejero, J. Hermoso, T. Mayoral, J. Sanz-Aparicio, K. Grever, and C. Gomez-Moreno Probing the Determinants of Coenzyme Specificity in Ferredoxin-NADP+ Reductase by Site-directed Mutagenesis J. Biol. Chem., April 6, 2001; 276(15): 11902 - 11912. [Abstract] [Full Text] [PDF]

				M. Vollmer, N. Thomsen, S. Wiek, and F. Seeber Apicomplexan Parasites Possess Distinct Nuclear-encoded, but Apicoplast-localized, Plant-type Ferredoxin-NADP+ Reductase and Ferredoxin J. Biol. Chem., February 16, 2001; 276(8): 5483 - 5490. [Abstract] [Full Text] [PDF]

				M. Martinez-Julvez, I. Nogues, M. Faro, J. K. Hurley, T. B. Brodie, T. Mayoral, J. Sanz-Aparicio, J. A. Hermoso, M. T. Stankovich, M. Medina, et al. Role of a Cluster of Hydrophobic Residues Near the FAD Cofactor in Anabaena PCC 7119 Ferredoxin-NADP+ Reductase for Optimal Complex Formation and Electron Transfer to Ferredoxin J. Biol. Chem., July 13, 2001; 276(29): 27498 - 27510. [Abstract] [Full Text] [PDF]

				A. K. Arakaki, E. G. Orellano, N. B. Calcaterra, J. Ottado, and E. A. Ceccarelli Involvement of the Flavin si-Face Tyrosine on the Structure and Function of Ferredoxin-NADP+ Reductases J. Biol. Chem., November 21, 2001; 276(48): 44419 - 44426. [Abstract] [Full Text] [PDF]