ArticleThe Journal of biological chemistry2010
Biochemical and spectroscopic characterization of the human mitochondrial amidoxime reducing components hmARC-1 and hmARC-2 suggests the existence of a new molybdenum enzyme family in eukaryotes.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers, 1 of them a synthesis that pooled it.
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Who cites it
50 citing papers in PubMed, 1 synthesis or guideline pooled it, 112 citations in OpenAlex.
- Effects of Passive or Active Recovery Regimes Applied During Long-Term Interval Training on Physical Fitness in Healthy Trained and Untrained Individuals: A Systematic Review.Sports medicine - open · 2024Pooled it
- Extracellular Vesicles, Nutrient Balance, and Redox Metabolism During Epididymal Sperm Maturation: A Perspective on the Complexity of Intercellular Interplay.Advances in anatomy, embryology, and cell biology · 2026Review
- Evolutionary-conserved RLF, a cytochrome bThe New phytologist · 2025Article
- Investigating the role of prognostic mitophagy-related genes in non-small cell cancer pathogenesis via multiomics and network-based approach.3 Biotech · 2024Article
- mARC1 Is the Main Contributor to Metabolic Reduction ofJournal of medicinal chemistry · 2024Article
- Second-Coordination-Sphere Effects Reveal Electronic Structure Differences between the Mitochondrial Amidoxime Reducing Component and Sulfite Oxidase.Inorganic chemistry · 2024Article
- Molybdenum's Role as an Essential Element in Enzymes Catabolizing Redox Reactions: A Review.Biomolecules · 2024Review
- Advancing Our Understanding of Pyranopterin-Dithiolene Contributions to Moco Enzyme Catalysis.Molecules (Basel, Switzerland) · 2023Review
- Reduction of Hydrogen Peroxide by Human Mitochondrial Amidoxime Reducing Component Enzymes.Molecules (Basel, Switzerland) · 2023Article
- The History of mARC.Molecules (Basel, Switzerland) · 2023Review
- Active Site Structures of theInorganic chemistry · 2023Article
- Spectroscopic Studies of Mononuclear Molybdenum Enzyme Centers.Molecules (Basel, Switzerland) · 2022Review
- Review
- Downregulation of MARC2 Promotes Immune Escape and Is Associated With Immunosuppression of Hepatocellular Carcinoma.Frontiers in genetics · 2021Article
- Article
- Functional mononuclear molybdenum enzymes: challenges and triumphs in molecular cloning, expression, and isolation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Review
- Molybdenum and Tungsten Cofactors and the Reactions They Catalyze.Metal ions in life sciences · 2020Article
- Molybdenum Enzymes and How They Support Virulence in Pathogenic Bacteria.Frontiers in microbiology · 2020Review
- Mitochondrial amidoxime-reducing component 2 (MARC2) has a significant role inThe Journal of biological chemistry · 2019Article
- DMSO Reductase Family: Phylogenetics and Applications of Extremophiles.International journal of molecular sciences · 2019Review
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mitochondrial amidoxime reducing component mARC is a newly discovered molybdenum enzyme that is presumed to form the catalytical part of a three-component enzyme system, consisting of mARC, heme/cytochrome b(5), and NADH/FAD-dependent cytochrome b(5) reductase. mARC proteins share a significant degree of homology to the molybdenum cofactor-binding domain of eukaryotic molybdenum cofactor sulfurase proteins, the latter catalyzing the post-translational activation of aldehyde oxidase and xanthine oxidoreductase. The human genome harbors two mARC genes, referred to as hmARC-1/MOSC-1 and hmARC-2/MOSC-2, which are organized in a tandem arrangement on chromosome 1. Recombinant expression of hmARC-1 and hmARC-2 proteins in Escherichia coli reveals that both proteins are monomeric in their active forms, which is in contrast to all other eukaryotic molybdenum enzymes that act as homo- or heterodimers. Both hmARC-1 and hmARC-2 catalyze the N-reduction of a variety of N-hydroxylated substrates such as N-hydroxy-cytosine, albeit with different specificities. Reconstitution of active molybdenum cofactor onto recombinant hmARC-1 and hmARC-2 proteins in the absence of sulfur indicates that mARC proteins do not belong to the xanthine oxidase family of molybdenum enzymes. Moreover, they also appear to be different from the sulfite oxidase family, because no cysteine residue could be identified as a putative ligand of the molybdenum atom. This suggests that the hmARC proteins and sulfurase represent members of a new family of molybdenum enzymes.
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