ArticleJournal of the American Chemical Society2015
Oxyl and hydroxyl radical transfer in mitochondrial amidoxime reducing component-catalyzed nitrite reduction.
Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Second-Coordination-Sphere Effects Reveal Electronic Structure Differences between the Mitochondrial Amidoxime Reducing Component and Sulfite Oxidase.Inorganic chemistry · 2024Article
- Active Site Characterization of aInorganic chemistry · 2024Article
- Advancing Our Understanding of Pyranopterin-Dithiolene Contributions to Moco Enzyme Catalysis.Molecules (Basel, Switzerland) · 2023Review
- Bringing Nitric Oxide to the Molybdenum World-A Personal Perspective.Molecules (Basel, Switzerland) · 2023Review
- Active Site Structures of theInorganic chemistry · 2023Article
- Spectroscopic Studies of Mononuclear Molybdenum Enzyme Centers.Molecules (Basel, Switzerland) · 2022Review
- 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
- Addressing Ligand-Based Redox in Molybdenum-Dependent Methionine Sulfoxide Reductase.Journal of the American Chemical Society · 2020Article
- Role of Nitrate Reductase in NO Production in Photosynthetic Eukaryotes.Plants (Basel, Switzerland) · 2019Review
- Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their RegulationPhysiological reviews · 2019Review
- Nitrite and nitrate chemical biology and signalling.British journal of pharmacology · 2019Review
- Submergence and Waterlogging Stress in Plants: A Review Highlighting Research Opportunities and Understudied Aspects.Frontiers in plant science · 2019Review
- From the Eukaryotic Molybdenum Cofactor Biosynthesis to the Moonlighting Enzyme mARC.Molecules (Basel, Switzerland) · 2018Review
- Integration between ROS Regulatory Systems and Other Signals in the Regulation of Various Types of Heat Responses in Plants.International journal of molecular sciences · 2018Review
- Putting xanthine oxidoreductase and aldehyde oxidase on the NO metabolism map: Nitrite reduction by molybdoenzymes.Redox biology · 2018Review
- Molybdenum-containing nitrite reductases: Spectroscopic characterization and redox mechanism.Redox report : communications in free radical research · 2017Review
- Understanding nitrate assimilation and its regulation in microalgae.Frontiers in plant science · 2015Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
A combination of electron paramagnetic resonance (EPR) spectroscopy and computational approaches has provided insight into the nature of the reaction coordinate for the one-electron reduction of nitrite by the mitochondrial amidoxime reducing component (mARC) enzyme. The results show that a paramagnetic Mo(V) species is generated when reduced enzyme is exposed to nitrite, and an analysis of the resulting EPR hyperfine parameters confirms that mARC is remarkably similar to the low-pH form of sulfite oxidase. Two mechanisms for nitrite reduction have been considered. The first shows a modest reaction barrier of 14 kcal/mol for the formation of ·NO from unprotonated nitrite substrate. In marked contrast, protonation of the substrate oxygen proximal to Mo in the Mo(IV)-O-N-O substrate-bound species results in barrierless conversion to products. A fragment orbital analysis reveals a high degree of Mo-O(H)-N-O covalency that provides a π-orbital pathway for one-electron transfer to the substrate and defines orbital constraints on the Mo-substrate geometry for productive catalysis in mARC and other pyranopterin molybdenum enzymes that catalyze this one-electron transformation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.