Structural and functional diversity of ferredoxin-NADP(+) reductases.
Arch Biochem Biophys
; 474(2): 283-91, 2008 Jun 15.
Article
en En
| MEDLINE
| ID: mdl-18307973
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.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Proteínas de Plantas
/
Modelos Moleculares
/
Ferredoxina-NADP Reductasa
/
Ferredoxinas
/
Glutatión Reductasa
/
NADP
Tipo de estudio:
Prognostic_studies
Límite:
Animals
Idioma:
En
Revista:
Arch Biochem Biophys
Año:
2008
Tipo del documento:
Article
País de afiliación:
Italia