ArticleJournal of the American Chemical Society2011
Spectroscopic and computational studies of α-keto acid binding to Dke1: understanding the role of the facial triad and the reactivity of β-diketones.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 24 citations in OpenAlex.
- Recent discoveries in mono- and dinuclear nonheme iron enzymes: Emerging mechanisms and catalytic strategies.Archives of biochemistry and biophysics · 2026Review
- Revisiting Reduction of COJACS Au · 2022Article
- NDalton transactions (Cambridge, England : 2003) · 2020Article
- Go it alone: four-electron oxidations by mononuclear non-heme iron enzymes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- Mono- and binuclear non-heme iron chemistry from a theoretical perspective.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Review
- An iron-oxygen intermediate formed during the catalytic cycle of cysteine dioxygenase.Chemical communications (Cambridge, England) · 2016Article
- Dioxygen reactivity of biomimetic Fe(II) complexes with noninnocent catecholate, o-aminophenolate, and o-phenylenediamine ligands.Inorganic chemistry · 2014Article
- Structure and function of atypically coordinated enzymatic mononuclear non-heme-Fe(II) centers.Coordination chemistry reviews · 2013Review
- Article
- Fe(II) complexes that mimic the active site structure of acetylacetone dioxygenase: O2 and NO reactivity.Inorganic chemistry · 2012Article
- Dke1--structure, dynamics, and function: a theoretical and experimental study elucidating the role of the binding site shape and the hydrogen-bonding network in catalysis.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012Article
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3 authors at 2 institutions in 2 countries.
Funding
Abstract
The O(2) activating mononuclear nonheme iron enzymes generally have a common facial triad (two histidine and one carboxylate (Asp or Glu) residue) ligating Fe(II) at the active site. Exceptions to this motif have recently been identified in nonheme enzymes, including a 3His triad in the diketone cleaving dioxygenase Dke1. This enzyme is used to explore the role of the facial triad in directing reactivity. A combination of spectroscopic studies (UV-vis absorption, MCD, and resonance Raman) and DFT calculations is used to define the nature of the binding of the α-keto acid, 4-hydroxyphenlpyruvate (HPP), to the active site in Dke1 and the origin of the atypical cleavage (C2-C3 instead of C1-C2) pattern exhibited by this enzyme in the reaction of α-keto acids with dioxygen. The reduced charge of the 3His triad induces α-keto acid binding as the enolate dianion, rather than the keto monoanion, found for α-keto acid binding to the 2His/1 carboxylate facial triad enzymes. The mechanistic insight from the reactivity of Dke1 with the α-keto acid substrate is then extended to understand the reaction mechanism of this enzyme with its native substrate, acac. This study defines a key role for the 2His/1 carboxylate facial triad in α-keto acid-dependent mononuclear nonheme iron enzymes in stabilizing the bound α-keto acid as a monoanion for its decarboxylation to provide the two additional electrons required for O(2) activation.
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