ArticleProceedings of the National Academy of Sciences of the United States of America2013
Organophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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36 citing papers in PubMed.
- Transition Metal Activation Reframes SAMHD1 Regulation.ACS chemical biology · 2026Article
- Thiooxazole Formation on a NontypeablebioRxiv : the preprint server for biology · 2026Article
- Transition metal activation reframes SAMHD1 regulation.bioRxiv : the preprint server for biology · 2026Article
- The Heme Oxygenase-Like Diiron Enzyme HrmI Reveals Altered Regulatory Mechanisms for Dioxygen Activation and Substrate N-Oxygenation.Journal of the American Chemical Society · 2025Article
- Discovery of a Two-Step Enzyme Cascade Converting Aspartate to Aminomalonate in Peptide Natural Product Biosynthesis.Journal of the American Chemical Society · 2025Article
- OJournal of the American Chemical Society · 2025Article
- Glyphosate-Induced Phosphonatase Operons in Soil Bacteria of the GenusInternational journal of molecular sciences · 2024Article
- Initial Steps in Methanobactin Biosynthesis: Substrate Binding by the Mixed-Valent Diiron Enzyme MbnBC.Biochemistry · 2024Article
- N-Cα Bond Cleavage Catalyzed by a Multinuclear Iron Oxygenase from a Divergent Methanobactin-like RiPP Gene Cluster.Journal of the American Chemical Society · 2024Article
- The Microbial Degradation of Natural and Anthropogenic Phosphonates.Molecules (Basel, Switzerland) · 2023Review
- Enzymatic Hydroxylation of Aliphatic C-H Bonds by a Mn/Fe Cofactor.Journal of the American Chemical Society · 2023Article
- Macrocyclization and Backbone Rearrangement During RiPP Biosynthesis by a SAM-Dependent Domain-of-Unknown-Function 692.ACS central science · 2023Article
- Enzymatic Hydroxylation of Aliphatic C-H Bonds by a Mn/Fe Cofactor.bioRxiv : the preprint server for biology · 2023Article
- Article
- β-Hydroxylation of α-amino-β-hydroxylbutanoyl-glycyluridine catalyzed by a nonheme hydroxylase ensures the maturation of caprazamycin.Communications chemistry · 2022Article
- Domain Fusion of Two Oxygenases Affords Organophosphonate Degradation in Pathogenic Fungi.Biochemistry · 2022Article
- A mixed-valent Fe(II)Fe(III) species converts cysteine to an oxazolone/thioamide pair in methanobactin biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Metal Dependence and Functional Diversity of Type I Cas3 Nucleases.Biochemistry · 2022Article
- Biosynthesis of fosfomycin in pseudomonads reveals an unexpected enzymatic activity in the metallohydrolase superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Enzymes, Reacting with Organophosphorus Compounds as Detoxifiers: Diversity and Functions.International journal of molecular sciences · 2021Review
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7 authors.
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Abstract
The founding members of the HD-domain protein superfamily are phosphohydrolases, and newly discovered members are generally annotated as such. However, myo-inositol oxygenase (MIOX) exemplifies a second, very different function that has evolved within the common scaffold of this superfamily. A recently discovered HD protein, PhnZ, catalyzes conversion of 2-amino-1-hydroxyethylphosphonate to glycine and phosphate, culminating a bacterial pathway for the utilization of environmentally abundant 2-aminoethylphosphonate. Using Mössbauer and EPR spectroscopies, X-ray crystallography, and activity measurements, we show here that, like MIOX, PhnZ employs a mixed-valent Fe(II)/Fe(III) cofactor for the O2-dependent oxidative cleavage of its substrate. Phylogenetic analysis suggests that many more HD proteins may catalyze yet-unknown oxygenation reactions using this hitherto exceptional Fe(II)/Fe(III) cofactor. The results demonstrate that the catalytic repertoire of the HD superfamily extends well beyond phosphohydrolysis and suggest that the mechanism used by MIOX and PhnZ may be a common strategy for oxidative C-X bond cleavage.
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