Your browser doesn't support javascript.
loading
Structural and functional diversity of ferredoxin-NADP(+) reductases.
Aliverti, Alessandro; Pandini, Vittorio; Pennati, Andrea; de Rosa, Matteo; Zanetti, Giuliana.
Afiliación
  • Aliverti A; Dipartimento di Scienze Biomolecolari e Biotecnologie, Università degli Studi di Milano, via Celoria 26, 20133 Milano, Italy. alessandro.aliverti@unimi.it
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.
Asunto(s)

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

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