Next Article in Journal
Fusaproliferin, a Fungal Mycotoxin, Shows Cytotoxicity against Pancreatic Cancer Cell Lines
Next Article in Special Issue
A Comparative Study of Molybdenum Carbonyl and Oxomolybdenum Derivatives Bearing 1,2,3-Triazole or 1,2,4-Triazole in Catalytic Olefin Epoxidation
Previous Article in Journal
Evolution of Volatile Compounds and Spoilage Bacteria in Smoked Bacon during Refrigeration Using an E-Nose and GC-MS Combined with Partial Least Squares Regression
Previous Article in Special Issue
Molybdenum-Catalyzed Enantioselective Sulfoxidation Controlled by a Nonclassical Hydrogen Bond between Coordinated Chiral Imidazolium-Based Dicarboxylate and Peroxido Ligands
Open AccessReview

From the Eukaryotic Molybdenum Cofactor Biosynthesis to the Moonlighting Enzyme mARC

Departamento de Bioquímica y Biología Molecular, Campus de Rabanales y Campus Internacional de Excelencia Agroalimentario (CeiA3), Edif. Severo Ochoa, Universidad de Córdoba, 14071 Cordoba, Spain
*
Author to whom correspondence should be addressed.
Molecules 2018, 23(12), 3287; https://doi.org/10.3390/molecules23123287
Received: 30 October 2018 / Revised: 23 November 2018 / Accepted: 5 December 2018 / Published: 11 December 2018
(This article belongs to the Special Issue Molybdenum-Catalyzed Oxidation Reactions)
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. View Full-Text
Keywords: molybdenum cofactor; mARC; moonlighting; nitrite; nitric oxide; cytochrome b5; nitrate reductase; NOFNiR; MOSC molybdenum cofactor; mARC; moonlighting; nitrite; nitric oxide; cytochrome b5; nitrate reductase; NOFNiR; MOSC
Show Figures

Graphical abstract

MDPI and ACS Style

Tejada-Jimenez, M.; Chamizo-Ampudia, A.; Calatrava, V.; Galvan, A.; Fernandez, E.; Llamas, A. From the Eukaryotic Molybdenum Cofactor Biosynthesis to the Moonlighting Enzyme mARC. Molecules 2018, 23, 3287.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Back to TopTop