ArticleBiochemistry2020
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).
Article in Biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 8 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
- Formation of Supramolecular Structures in Oxidation Processes Catalyzed by Heteroligand Complexes of Iron and Nickel: Models of Enzymes.International journal of molecular sciences · 2025Article
- Selective Catalysis by Complexes Including Ni and Redox-Inactive Alkali Metals (Li, Na, or K) in Oxidation Processes: The Role of Hydrogen Bonds and Supramolecular Structures.International journal of molecular sciences · 2025Article
- Dioxygenase Chemistry in Nucleophilic Aldehyde Deformylations Utilizing Dicopper OJournal of the American Chemical Society · 2024Article
- Tracking protein-protein interactions by NMR: conformational selection in human steroidogenic cytochrome P450 CYP17A1 induced by cytochromePhysical chemistry chemical physics : PCCP · 2024Article
- The Role H-Bonding and Supramolecular Structures in Homogeneous and Enzymatic Catalysis.International journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The metalloenzyme acireductone dioxygenase (ARD) shows metal-dependent physical and enzymatic activities depending upon the metal bound in the active site. The Fe(II)-bound enzyme catalyzes the penultimate step of the methionine salvage pathway, converting 1,2-dihydroxy-5-(methylthio)pent-1-en-3-one (acireductone) into formate and the ketoacid precursor of methionine, 2-keto-4-thiomethyl-2-oxobutanoate, using O
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