Cited by 937Metal-Catalyzed Oxygenation MechanismsEnzyme Structure and FunctionBiochemical Acid Research Studies

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Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes

Hausinger, Robert P.·2004·Critical Reviews in Biochemistry and Molecular Biology

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Abstract

FeII/alpha-ketoglutarate (alphaKG)-dependent hydroxylases catalyze an amazing diversity of reactions that result in protein side-chain modifications, repair of alkylated DNA/RNA, biosynthesis of antibiotics and plant products, metabolism related to lipids, and biodegradation of a variety of compounds. These enzymes possess a beta-strand "jellyroll" structural fold that contains three metal-binding ligands found in a His1-X-Asp/Glu-Xn-His2 motif. The cosubstrate, alphaKG, chelates FeII using its C-2 keto group (binding opposite the Asp/Glu residue) and C-1 carboxylate (coordinating opposite either His1 or His2). Oxidative decomposition of alphaKG forms CO2 plus succinate and leads to the generation of an FeIV-oxo or other activated oxygen species that hydroxylate the primary substrate. The reactive oxygen species displays alternate reactivity in related enzymes that catalyze desaturations, ring expansions, or ring closures. Other enzymes resemble the FeII/alphaKG-dependent hydroxylases in terms of protein structure or chemical mechanism but do not utilize alphaKG as a substrate. This review describes the reactions catalyzed by this superfamily of enzymes, highlights key active site features revealed by structural studies, and summarizes results from spectroscopic and other approaches that provide insights into the chemical mechanisms.

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Authors: Hausinger, R. P.
Affiliations: Michigan State University (US)
Corresponding author: Hausinger, Robert P.
ORCID: Hausinger, Robert P.
Venue: Critical Reviews in Biochemistry and Molecular Biology
Publisher: Informa UK Limited
Published: 2004-01
Volume: 39
Issue: 1
Pages: 21-68
ISSN: 0045-6411 (ISSN-L)
1040-9238
1549-7798
DOI: 10.1080/10409230490440541
OpenAlex: W2128586767
Cited by: 937
References: 335
Citations by year: 2026: 37 · 2025: 27 · 2024: 42 · 2023: 34 · 2022: 41 · 2021: 56 · 2020: 45 · 2019: 44 · 2018: 43 · 2017: 44 · 2016: 44 · 2015: 67 · 2014: 60 · 2013: 48 · 2012: 48
FWCI: 25.19
Type: journal article
Language: en
Open access: closed
Locations: Critical Reviews in Biochemistry and Molecular Biology (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of General Medical Sciences (GM063584, R01GM063584)
Topics: Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Biochemical Acid Research Studies
Keywords: alpha-ketoglutarate, reactive oxygen species, DNA repair, alkylated DNA, antibiotic biosynthesis, lipid metabolism, biodegradation, desaturation, ring expansion, cyclization, active site structure, enzyme mechanism
MeSH terms: Ferrous Compounds, Mixed Function Oxygenases, Ketoglutaric Acids, Protein Conformation, Molecular Structure

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Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes

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