ArticleEukaryotic cell2011
The Chlamydomonas reinhardtii molybdenum cofactor enzyme crARC has a Zn-dependent activity and protein partners similar to those of its human homologue.
Article in Eukaryotic cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 49 citations in OpenAlex.
- The Mechanisms of Molybdate Distribution and Homeostasis with Special Focus on the Model PlantMolecules (Basel, Switzerland) · 2023Review
- Reduction of Hydrogen Peroxide by Human Mitochondrial Amidoxime Reducing Component Enzymes.Molecules (Basel, Switzerland) · 2023Article
- Review
- Role of Nitrate Reductase in NO Production in Photosynthetic Eukaryotes.Plants (Basel, Switzerland) · 2019Review
- From the Eukaryotic Molybdenum Cofactor Biosynthesis to the Moonlighting Enzyme mARC.Molecules (Basel, Switzerland) · 2018Review
- Crystal structure of human mARC1 reveals its exceptional position among eukaryotic molybdenum enzymes.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Study of Different Variants of Mo Enzyme crARC and the Interaction with Its Partners crCytb5-R and crCytb5-1.International journal of molecular sciences · 2017Article
- Beyond Tryptophan Synthase: Identification of Genes That Contribute to Chlamydia trachomatis Survival during Gamma Interferon-Induced Persistence and Reactivation.Infection and immunity · 2016Article
- The mammalian molybdenum enzymes of mARC.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Review
- Nitrite reductase and nitric-oxide synthase activity of the mitochondrial molybdopterin enzymes mARC1 and mARC2.The Journal of biological chemistry · 2014Article
- Molybdenum metabolism in plants and crosstalk to iron.Frontiers in plant science · 2014Review
- TusA (YhhP) and IscS are required for molybdenum cofactor-dependent base-analog detoxification.MicrobiologyOpen · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ARC (amidoxime reducing component) proteins are molybdenum cofactor (Moco) enzymes named hmARC1 and hmARC2 (human ARCs [hmARCs]) in humans and YcbX in Escherichia coli. They catalyze the reduction of a broad range of N-hydroxylated compounds (NHC) using reducing power supplied by other proteins. Some NHC are prodrugs or toxic compounds. YcbX contains a ferredoxin (Fd) domain and requires the NADPH flavin reductase CysJ to reduce NHC. In contrast, hmARCs lack the Fd domain and require a human cytochrome b5 (hCyt b5) and a human NADH Cyt b5 reductase (hCyt b5-R) to reduce NHC. The ARC proteins in the plant kingdom are uncharacterized. We demonstrate that Chlamydomonas reinhardtii mutants defective in Moco biosynthesis genes are sensitive to the NHC N(6)-hydroxylaminopurine (HAP). The Chlamydomonas reinhardtii ARC protein crARC has been purified and characterized. The six Chlamydomonas Fds were isolated, but none of them are required by crARC to reduce HAP. We have also purified and characterized five C. reinhardtii Cyt b5 (crCyt b5) and two flavin reductases, one that is NADPH dependent (crCysJ) and one that is NADH dependent (crCyt b5-R). The data show that crARC uses crCyt b5-1 and crCyt b5-R to reduce HAP. The crARC has a Zn-dependent activity, and the presence of Zn increases its V(max) more than 14-fold. In addition, all five cysteines of crARC were substituted by alanine, and we demonstrate that the fully conserved cysteine 252 is essential for both Moco binding and catalysis. Therefore, it is proposed that crARC belongs to the sulfite oxidase family of Moco enzymes.
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