ArticleBiochemistry2016
Metal-Dependent Function of a Mammalian Acireductone Dioxygenase.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 42 citations in OpenAlex.
- Discovery of a phenazine-thiol conjugase from sparse data using genome-informed machine learning.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Discovery of a phenazine-thiol conjugase from sparse data using genome-informed machine learning.bioRxiv : the preprint server for biology · 2026Article
- Tetrad or triad? insights from a versatile Fe(ii) structural and functional model of the 3-histidine 1-carboxylate tetrad in C-C bond cleaving dioxygenase enzymes.RSC advances · 2026Article
- Design of a protein scaffold with a selective, Bi-containing heterodinuclear metal coordination motif.Journal of inorganic biochemistry · 2026Article
- Harnessing Oxidizing Potential of Nickel for Sustainable Hydrocarbon Functionalization.Molecules (Basel, Switzerland) · 2024Review
- Unraveling the Pivotal Roles of Various Metal Ion Centers in the Catalysis of Quercetin 2,4-Dioxygenases.Molecules (Basel, Switzerland) · 2023Article
- Aldolase B attenuates clear cell renal cell carcinoma progression by inhibiting CtBP2.Frontiers of medicine · 2023Article
- Five decades of metalloenzymology.The Enzymes · 2023Review
- Interchangeable utilization of metals: New perspectives on the impacts of metal ions employed in ancient and extant biomolecules.The Journal of biological chemistry · 2021Review
- Article
- A Model for the Solution Structure of Human Fe(II)-Bound Acireductone Dioxygenase and Interactions with the Regulatory Domain of Matrix Metalloproteinase I (MMP-I).Biochemistry · 2020Article
- A family of structural and functional models for the active site of a unique dioxygenase: Acireductone dioxygenase (ARD).Journal of inorganic biochemistry · 2020Article
- Structure, function, and biosynthesis of nickel-dependent enzymes.Protein science : a publication of the Protein Society · 2020Review
- Human acireductone dioxygenase (HsARD), cancer and human health: Black hat, white hat or gray?Inorganics · 2019Article
- Overexpression ofFrontiers in plant science · 2019Article
- On the Structure and Reaction Mechanism of Human Acireductone Dioxygenase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2018Article
- The Metal Drives the Chemistry: Dual Functions of Acireductone Dioxygenase.Chemical reviews · 2017Review
- The hidden treasure in your data: phasing with unexpected weak anomalous scatterers from routine data sets.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Oxygen activation by mononuclear Mn, Co, and Ni centers in biology and synthetic complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- Dual chemistry catalyzed by human acireductone dioxygenase.Protein engineering, design & selection : PEDS · 2017Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The two acireductone dioxygenase (ARD) isozymes from the methionine salvage pathway of Klebsiella oxytoca are the only known pair of naturally occurring metalloenzymes with distinct chemical and physical properties determined solely by the identity of the divalent transition metal ion (Fe(2+) or Ni(2+)) in the active site. We now show that this dual chemistry can also occur in mammals. ARD from Mus musculus (MmARD) was studied to relate the metal ion identity and three-dimensional structure to enzyme function. The iron-containing isozyme catalyzes the cleavage of 1,2-dihydroxy-3-keto-5-(thiomethyl)pent-1-ene (acireductone) by O2 to formate and the ketoacid precursor of methionine, which is the penultimate step in methionine salvage. The nickel-bound form of ARD catalyzes an off-pathway reaction resulting in formate, carbon monoxide (CO), and 3-(thiomethyl) propionate. Recombinant MmARD was expressed and purified to obtain a homogeneous enzyme with a single transition metal ion bound. The Fe(2+)-bound protein, which shows about 10-fold higher activity than that of others, catalyzes on-pathway chemistry, whereas the Ni(2+), Co(2+), or Mn(2+) forms exhibit off-pathway chemistry, as has been seen with ARD from Klebsiella. Thermal stability of the isozymes is strongly affected by the metal ion identity, with Ni(2+)-bound MmARD being the most stable, followed by Co(2+) and Fe(2+), and Mn(2+)-bound ARD being the least stable. Ni(2+)- and Co(2+)-bound MmARD were crystallized, and the structures of the two proteins found to be similar. Enzyme-ligand complexes provide insight into substrate binding, metal coordination, and the catalytic mechanism.
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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.