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This minireview covers the research carried out in recent years into differ-ent aspects of the function of the flavoproteins involved in cyanobacterial photosynthetic electron transfer from photosystem I to NADP + , flavodox-in and ferredoxin–NADP + reductase. Interactions that stabilize protein– flavin complexes and tailor the midpoint potentials in these proteins, as well as many details of the binding and electron transfer to protein and ligand partners, have been revealed. | MINIREVIEW Structural and mechanistic aspects of flavoproteins photosynthetic electron transfer from photosystem I to NADP Milagros Medina Departamento de Bioquimica y Biologia Molecular y Celular and BFIF Universidad de Zaragoza Spain Keywords electron transfer ferredoxin ferredoxin-NADP reductase flavodoxin hydride transfer NAD P H photosystem I protein-flavin complexes protein-protein and protein-ligand interaction redox potential regulation Correspondence M. Medina Departamento de Bioquimica y Biologia Molecular y Celular Facultad de Ciencias Pedro Cerbuna 12 Universidad de Zaragoza 50009-Zaragoza Spain Fax 34 976 762123 Tel 34 976 762476 E-mail mmedina@unizar.es Received 28 January 2009 revised 22 April2009 accepted 4 May 2009 doi 10.1111 j.1742-4658.2009.07122.x This minireview covers the research carried out in recent years into different aspects of the function of the flavoproteins involved in cyanobacterial photosynthetic electron transfer from photosystem I to NADP flavodox-in and ferredoxin-NADP reductase. Interactions that stabilize protein-flavin complexes and tailor the midpoint potentials in these proteins as well as many details of the binding and electron transfer to protein and ligand partners have been revealed. In addition to their role in photosynthesis flavodoxin and ferredoxin-NADP reductase are ubiquitous fla-voenzymes that deliver NAD P H or low midpoint potential one-electron donors to redox-based metabolisms in plastids mitochondria and bacteria. They are also the basic prototypes for a large family of diflavin electron transferases with common functional and structural properties. Understanding their mechanisms should enable greater comprehension of the many physiological roles played by flavodoxin and ferredoxin-NADP reductase either free or as modules in multidomain proteins. Many aspects of their biochemistry have been extensively characterized using a combination of site-directed mutagenesis steady-state and transient kinetics .
