ArticleJournal of the American Chemical Society2011
Insights into the different dioxygen activation pathways of methane and toluene monooxygenase hydroxylases.
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 17 papers.
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Who cites it
17 citing papers in PubMed, 46 citations in OpenAlex.
- Structural and functional fine mapping of cysteines in mammalian glutaredoxin reveal their differential oxidation susceptibility.Nature communications · 2023Article
- Second Coordination Sphere Effects on the Mechanistic Pathways for Dioxygen Activation by a Ferritin: Involvement of a Tyr Radical and the Identification of a Cation Binding Site.Chembiochem : a European journal of chemical biology · 2022Article
- Understanding desaturation/hydroxylation activity of castor stearoyl ΔComputational and structural biotechnology journal · 2022Article
- Ligand-Constraint-Induced Peroxide Activation for Electrophilic Reactivity.Angewandte Chemie (International ed. in English) · 2021Article
- A nonheme peroxo-diiron(III) complex exhibiting both nucleophilic and electrophilic oxidation of organic substrates.Dalton transactions (Cambridge, England : 2003) · 2021Article
- Proton-Electron Transfer to the Active Site Is Essential for the Reaction Mechanism of Soluble ΔJournal of the American Chemical Society · 2020Article
- Characterization of toluene metabolism by methanotroph and its effect on methane oxidation.Environmental science and pollution research international · 2018Article
- Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes.Chemical reviews · 2018Review
- Unprecedented (μ-1,1-Peroxo)diferric Structure for the Ambiphilic Orange Peroxo Intermediate of the Nonheme N-Oxygenase CmlI.Journal of the American Chemical Society · 2017Article
- Peroxide Activation for Electrophilic Reactivity by the Binuclear Non-heme Iron Enzyme AurF.Journal of the American Chemical Society · 2017Article
- Protein effects in non-heme iron enzyme catalysis: insights from multiscale models.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Review
- X-ray absorption spectroscopic characterization of the diferric-peroxo intermediate of human deoxyhypusine hydroxylase in the presence of its substrate eIF5a.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- 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
- Evolution of strategies to prepare synthetic mimics of carboxylate-bridged diiron protein active sites.Journal of inorganic biochemistry · 2011Review
- Characterization of a synthetic peroxodiiron(III) protein model complex by nuclear resonance vibrational spectroscopy.Chemical communications (Cambridge, England) · 2011Article
- Mechanistic studies of reactions of peroxodiiron(III) intermediates in T201 variants of toluene/o-xylene monooxygenase hydroxylase.Biochemistry · 2011Article
- Dioxygen activation in soluble methane monooxygenase.Accounts of chemical research · 2011Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The methane and toluene monooxygenase hydroxylases (MMOH and TMOH, respectively) have almost identical active sites, yet the physical and chemical properties of their oxygenated intermediates, designated P*, H(peroxo), Q, and Q* in MMOH and ToMOH(peroxo) in a subclass of TMOH, ToMOH, are substantially different. We review and compare the structural differences in the vicinity of the active sites of these enzymes and discuss which changes could give rise to the different behavior of H(peroxo) and Q. In particular, analysis of multiple crystal structures reveals that T213 in MMOH and the analogous T201 in TMOH, located in the immediate vicinity of the active site, have different rotatory configurations. We study the rotational energy profiles of these threonine residues with the use of molecular mechanics (MM) and quantum mechanics/molecular mechanics (QM/MM) computational methods and put forward a hypothesis according to which T213 and T201 play an important role in the formation of different types of peroxodiiron(III) species in MMOH and ToMOH. The hypothesis is indirectly supported by the QM/MM calculations of the peroxodiiron(III) models of ToMOH and the theoretically computed Mössbauer spectra. It also helps explain the formation of two distinct peroxodiiron(III) species in the T201S mutant of ToMOH. Additionally, a role for the ToMOD regulatory protein, which is essential for intermediate formation and protein functioning in the ToMO system, is advanced. We find that the low quadrupole splitting parameter in the Mössbauer spectrum observed for a ToMOH(peroxo) intermediate can be explained by protonation of the peroxo moiety, possibly stabilized by the T201 residue. Finally, similarities between the oxygen activation mechanisms of the monooxygenases and cytochrome P450 are discussed.
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