• Title of article

    Structural and functional diversity of ferredoxin-NADP+ reductases

  • Author/Authors

    Aliverti، نويسنده , , Alessandro and Pandini، نويسنده , , Vittorio and Pennati، نويسنده , , Andrea and de Rosa، نويسنده , , Matteo and Zanetti، نويسنده , , Giuliana، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2008
  • Pages
    9
  • From page
    283
  • To page
    291
  • Abstract
    Although all ferredoxin-NADP+ reductases (FNRs) catalyze the same reaction, i.e. the transfer of reducing equivalents between NADP(H) and ferredoxin, they belong to two unrelated families of proteins: the plant-type and the glutathione reductase-type of FNRs. Aim of this review is to provide a general classification scheme for these enzymes, to be used as a framework for the comparison of their properties. Furthermore, we report on some recent findings, which significantly increased the understanding of the structure–function relationships of FNRs, i.e. the ability of adrenodoxin reductase and its homologs to catalyze the oxidation of NADP+ to its 4-oxo derivative, and the properties of plant-type FNRs from non-photosynthetic organisms. Plant-type FNRs from bacteria and Apicomplexan parasites provide examples of novel ways of FAD- and NADP(H)-binding. The recent characterization of an FNR from Plasmodium falciparum brings these enzymes into the field of drug design.
  • Keywords
    Apicomplexa , malaria , FAD , flavoprotein , NADP , Electron transfer , induced fit , Plasmodium Falciparum , Photosynthesis
  • Journal title
    Archives of Biochemistry and Biophysics
  • Serial Year
    2008
  • Journal title
    Archives of Biochemistry and Biophysics
  • Record number

    1629487