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
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