Academic Journal

Structural and functional diversity of ferredoxin-NADP+ reductases

التفاصيل البيبلوغرافية
العنوان: Structural and functional diversity of ferredoxin-NADP+ reductases
المؤلفون: A. Aliverti, V. Pandini, A. Pennati, M. de Rosa, G. Zanetti
المساهمون: A. Aliverti, V. Pandini, A. Pennati, M. de Rosa, G. Zanetti
بيانات النشر: Elsevier Science
سنة النشر: 2008
المجموعة: The University of Milan: Archivio Istituzionale della Ricerca (AIR)
مصطلحات موضوعية: flavoprotein, FAD, NADP, photosynthesi, induced fit, electron transfer, Apicomplexa, Plasmodium falciparum, malaria, Settore BIO/10 - Biochimica
الوصف: 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.
نوع الوثيقة: article in journal/newspaper
اللغة: English
Relation: info:eu-repo/semantics/altIdentifier/pmid/18307973; info:eu-repo/semantics/altIdentifier/wos/WOS:000256691200007; Trends in Enzymology Conference; volume:474; issue:2; firstpage:283; lastpage:291; numberofpages:9; journal:ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS; http://hdl.handle.net/2434/41439; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-44549083194
DOI: 10.1016/j.abb.2008.02.014
الاتاحة: http://hdl.handle.net/2434/41439
https://doi.org/10.1016/j.abb.2008.02.014
Rights: info:eu-repo/semantics/openAccess
رقم الانضمام: edsbas.7F26C755
قاعدة البيانات: BASE
الوصف
DOI:10.1016/j.abb.2008.02.014