Structural and functional diversity of ferredoxin-NADP⁺ reductases

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• 作者：Aless ; ro Aliverti ; Vittorio P ; ini ; Andrea Pennati ; Matteo de Rosa ; Giuliana Zanetti
• 关键词：Flavoprotein ; FAD ; NADP ; Photosynthesis ; Induced fit ; Electron transfer ; Apicomplexa ; Plasmodium falciparum ; Malaria
• 刊名：Archives of Biochemistry and Biophysics
• 出版年：2008
• 出版时间：15 June 2008
• 年：2008
• 卷：474
• 期：2
• 页码：283-291
• 全文大小：1214 K

文摘

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.