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Archives of Biochemistry and Biophysics
Article . 2008 . Peer-reviewed
License: Elsevier TDM
Data sources: Crossref
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Structural and functional diversity of ferredoxin-NADP+ reductases

Authors: A. Aliverti; V. Pandini; A. Pennati; M. de Rosa; G. Zanetti;

Structural and functional diversity of ferredoxin-NADP+ reductases

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.

Country
Italy
Related Organizations
Keywords

Models, Molecular, Protein Conformation, Plasmodium falciparum, Protozoan Proteins, Catalysis, flavoprotein; FAD; NADP; photosynthesis; induced fit; electron transfer; Apicomplexa; Plasmodium falciparum; malaria, Electron Transport, Ferredoxin-NADP Reductase, Structure-Activity Relationship, Glutathione Reductase, Bacterial Proteins, Consensus Sequence, Animals, Ferredoxins, Amino Acid Sequence, NADP, Plant Proteins, Protein Binding

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
141
Top 10%
Top 10%
Top 1%
Green
bronze