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Showing 1 to 10 of 10 for “"dioxygen activation"”.
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A Reduced Oxy Intermediate of Cytochrome P450(cam) Involved in Dioxygen Activation
… involved in hydrocarbon hydroxylation and dioxygen activation have been precluded by the reduction of the oxy intermediate being the rate determining step. D251N cytochrome P450$\sb{\rm cam}$ slowed the overall catalytic rate, while maintaining full catalytic coupling, while exhibiting a …
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Auxiliary proton-influenced metal-mediated reactions: dioxygen activation, anion coordination, and catalysis
… and acid. The reactivity with dioxygen requires the hydroxyl substituent: neither [Cu(tripic)(NCMe)]+ nor the methoxy complexes display O2 reactivity. A similar mixed valence dimer was found to form upon exposing the dicopper(I) complex of a tetrahydroxy bis(tridentate) ligand …
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Dioxygen activation and substrate hydroxylation by the hydroxylase component of toluene/O-xylene monooxygenase from pseudomonas sporium OX1
… bacterial multicomponent monooxygenases activate dioxygen at structurally homologous active sites. Catalysis requires the management of four substrates: electrons, protons, dioxygen, and hydrocarbons. Protein component complexes control the delivery of these substrates to the diiron center in the …
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Advances in non-heme diiron modeling chemistry : developing functional protein mimics through ligand design and understanding dioxygen activation
… Complexes 1 and 2 both react rapidly with dioxygen. Oxygenation of 1 afforded a ([mu]-hydroxo)diiron(III) complex [Fe2([mu]- OH)(PIM)(Ph3CCO2)3] (4), a hexa([mu]-hydroxo)tetrairon(III) complex [Fe4([mu]- OH)6(PIM)2(Ph3CCO2)2] (5), and an unidentified iron(III) species. Oxygenation of 2 …
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Understanding orchestrated chemical reactions in toluene/o-xylene monooxygenase from pseudomonas sporium OX1
… a carboxylate-bridged non-heme diiron motif for dioxygen activation. Despite their conserved diiron active site structures and mechanisms of dioxygen activation, they catalyze a wide range of chemical transformations. These observations suggest that diiron-containing enzymes have distinct active …
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Exploring reactivity and component interactions in Toluene/o-Xylene Monooxygenase from pseudomonas sp. OX1
… oxidation of hydrocarbon substrates through activation of dioxygen. Each BMM utilizes a diiron active site housed within a catalytic hydroxylase protein. This diiron active site is responsible for activation of dioxygen and oxidation of hydrocarbons. Additional component proteins modify the …
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Modeling the active sites of non-heme diiron metalloproteins with sterically hindered carboxylates and syn N-Donor ligands
… non-heme diiron enzymes activate dioxygen to perform a variety of biological functions. Synthetic model compounds have been prepared to gain insight into the intricacies of dioxygen activation in these enzymes. In this introductory chapter, the challenges and advances of different …
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Bio-inspired iron complexes featuring secondary coordination sphere interactions: Ligand design strategies and dioxygen reactivity
The activation of dioxygen plays an important role in processes ranging from biological oxidation to energy storage and utilization. In Nature, metalloenzymes use complex architectures to promote these multi-electron and multi-proton reactions using first-row transition metal centers. Many enzymes …
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Exploring the reactivity of bacterial multicomponent monooxygenases
… presents the proposed mechanisms of 02 activation by BMMs and related carboxylate-bridged diiron proteins, and discuses substrate reactivity of the oxygenated diiron units responsible for BMM catalysis. Chapter 2. Revisiting the Mechanism of Dioxygen Activation in Soluble Methane …
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Development & characterization of bio-inspired earth-abundant metal systems and extreme ultraviolet spectroscopy of precious metal photocatalysts
Submission published under a 24 month embargo labeled 'U of I Access', the embargo will last until 2024-08-01