ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2017
Go it alone: four-electron oxidations by mononuclear non-heme iron enzymes.
Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2017. 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, 47 citations in OpenAlex.
- Redox and Spin States Series of an Organometallic Heme Analogue Based on a Non-Innocent NHC/N-Donor Hybrid Macrocycle.Inorganic chemistry · 2026Article
- Influence of the second coordination sphere on OJournal of inorganic biochemistry · 2025Article
- Structural Basis for Methine Excision by a Heme Oxygenase-like Enzyme.ACS central science · 2024Article
- Multinuclear non-heme iron dependent oxidative enzymes (MNIOs) involved in unusual peptide modifications.Current opinion in chemical biology · 2024Review
- The Role of Sulfhydryl (Thiols) Groups in Oral and Periodontal Diseases.Biomedicines · 2024Article
- Role of dietary iron revisited: in metabolism, ferroptosis and pathophysiology of cancer.American journal of cancer research · 2022Review
- Characterization and chemical reactivity of room-temperature-stable MnChemical science · 2021Article
- Structurally Modelling the 2-His-1-Carboxylate Facial Triad with a Bulky N,N,O Phenolate Ligand.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Nonheme iron-thiolate complexes as structural models of sulfoxide synthase active sites.Dalton transactions (Cambridge, England : 2003) · 2020Article
- C-H Bond Cleavage Is Rate-Limiting for Oxidative C-P Bond Cleavage by the Mixed Valence Diiron-Dependent Oxygenase PhnZ.Biochemistry · 2019Article
- Roles of 2-oxoglutarate oxygenases and isopenicillin N synthase in β-lactam biosynthesis.Natural product reports · 2018Review
- Dioxygen activation by nonheme iron enzymes with the 2-His-1-carboxylate facial triad that generate high-valent oxoiron oxidants.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
This review discusses the current mechanistic understanding of a group of mononuclear non-heme iron-dependent enzymes that catalyze four-electron oxidation of their organic substrates without the use of any cofactors or cosubstrates. One set of enzymes acts on α-ketoacid-containing substrates, coupling decarboxylation to oxygen activation. This group includes 4-hydroxyphenylpyruvate dioxygenase, 4-hydroxymandelate synthase, and CloR involved in clorobiocin biosynthesis. A second set of enzymes acts on substrates containing a thiol group that coordinates to the iron. This group is comprised of isopenicillin N synthase, thiol dioxygenases, and enzymes involved in the biosynthesis of ergothioneine and ovothiol. The final group of enzymes includes HEPD and MPnS that both carry out the oxidative cleavage of the carbon-carbon bond of 2-hydroxyethylphosphonate but generate different products. Commonalities amongst many of these enzymes are discussed and include the initial substrate oxidation by a ferric-superoxo-intermediate and a second oxidation by a ferryl species.
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