ArticleChemistry (Weinheim an der Bergstrasse, Germany)2018
On the Structure and Reaction Mechanism of Human Acireductone Dioxygenase.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 28 citations in OpenAlex.
- 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
- BTG13-related metalloenzymes: Atypical non-heme iron-dependent dioxygenases with unusual coordination patterns and catalytic mechanisms.Engineering microbiology · 2025Review
- Dioxygenase Chemistry in Nucleophilic Aldehyde Deformylations Utilizing Dicopper OJournal of the American Chemical Society · 2024Article
- Unraveling the Pivotal Roles of Various Metal Ion Centers in the Catalysis of Quercetin 2,4-Dioxygenases.Molecules (Basel, Switzerland) · 2023Article
- Five decades of metalloenzymology.The Enzymes · 2023Review
- 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
- The metal- and substrate-dependences of 2,4'-dihydroxyacetophenone dioxygenase.Archives of biochemistry and biophysics · 2020Article
- Structure, function, and biosynthesis of nickel-dependent enzymes.Protein science : a publication of the Protein Society · 2020Review
- Regioselectivity of hyoscyamine 6β-hydroxylase-catalysed hydroxylation as revealed by high-resolution structural information and QM/MM calculations.Dalton transactions (Cambridge, England : 2003) · 2020Article
- Molstack: A platform for interactive presentations of electron density and cryo-EM maps and their interpretations.Protein science : a publication of the Protein Society · 2020Article
- Human acireductone dioxygenase (HsARD), cancer and human health: Black hat, white hat or gray?Inorganics · 2019Article
- Advances in Sustainable Catalysis: A Computational Perspective.Frontiers in chemistry · 2019Review
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 3 countries.
Funding
Abstract
Acireductone dioxygenase (ARD) is an intriguing enzyme from the methionine salvage pathway that is capable of catalysing two different oxidation reactions with the same substrate depending on the type of the metal ion in the active site. To date, the structural information regarding the ARD-acireductone complex is limited and possible reaction mechanisms are still under debate. The results of joint experimental and computational studies undertaken to advance knowledge about ARD are reported. The crystal structure of an ARD from Homo sapiens was determined with selenomethionine. EPR spectroscopy suggested that binding acireductone triggers one protein residue to dissociate from Fe
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