Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 474, Issue 2, Pages 283-291Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2008.02.014
Keywords
flavoprotein; FAD; NADP; photosynthesis; induced fit; electron transfer; Apicomplexa; Plasmodium falciparum; malaria
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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. (c) 2008 Elsevier Inc. All rights reserved.
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