• español
    • English
  • English 
    • español
    • English
  • Login
View Item 
  •   DSpace Home
  • Producción Científica
  • Artículos, capítulos, libros...UCO
  • View Item
  •   DSpace Home
  • Producción Científica
  • Artículos, capítulos, libros...UCO
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

From the Eukaryotic Molybdenum Cofactor Biosynthesis to the Moonlighting Enzyme mARC

Thumbnail
View/Open
molecules-23-03287-v2.pdf (1.298Mb)
Author
Tejada Jiménez, M.
Chamizo-Ampudia, Alejandro
Calatrava, Victoria
Galván Cejudo, Aurora
Fernández Reyes, Emilio
Llamas Azúa, Ángel
Publisher
MDPI
Date
2018
Subject
Molybdenum cofactor
mARC
Moonlighting
Nitrite
Nitric oxide
Cytochrome b5
Nitrate reductase
NOFNiR
MOSC
METS:
Mostrar el registro METS
PREMIS:
Mostrar el registro PREMIS
Metadata
Show full item record
Abstract
All eukaryotic molybdenum (Mo) enzymes contain in their active site a Mo Cofactor (Moco), which is formed by a tricyclic pyranopterin with a dithiolene chelating the Mo atom. Here, the eukaryotic Moco biosynthetic pathway and the eukaryotic Moco enzymes are overviewed, including nitrate reductase (NR), sulfite oxidase, xanthine oxidoreductase, aldehyde oxidase, and the last one discovered, the moonlighting enzyme mitochondrial Amidoxime Reducing Component (mARC). The mARC enzymes catalyze the reduction of hydroxylated compounds, mostly N-hydroxylated (NHC), but as well of nitrite to nitric oxide, a second messenger. mARC shows a broad spectrum of NHC as substrates, some are prodrugs containing an amidoxime structure, some are mutagens, such as 6-hydroxylaminepurine and some others, which most probably will be discovered soon. Interestingly, all known mARC need the reducing power supplied by different partners. For the NHC reduction, mARC uses cytochrome b5 and cytochrome b5 reductase, however for the nitrite reduction, plant mARC uses NR. Despite the functional importance of mARC enzymatic reactions, the structural mechanism of its Moco-mediated catalysis is starting to be revealed. We propose and compare the mARC catalytic mechanism of nitrite versus NHC reduction. By using the recently resolved structure of a prokaryotic MOSC enzyme, from the mARC protein family, we have modeled an in silico three-dimensional structure of a eukaryotic homologue.
URI
http://hdl.handle.net/10396/18056
Fuente
Molecules 23(12), 3287 (2018)
Versión del Editor
http://dx.doi.org/10.3390/molecules23123287
Collections
  • ceiA3
  • DBBM-Artículos, capítulos...
  • Artículos, capítulos, libros...UCO

DSpace software copyright © 2002-2015  DuraSpace
Contact Us | Send Feedback
© Biblioteca Universidad de Córdoba
Biblioteca  UCODigital
 

 

Browse

All of DSpaceCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects

My Account

LoginRegister

Statistics

View Usage Statistics

De Interés

Archivo Delegado/AutoarchivoAyudaPolíticas de Helvia

Compartir


DSpace software copyright © 2002-2015  DuraSpace
Contact Us | Send Feedback
© Biblioteca Universidad de Córdoba
Biblioteca  UCODigital