A N3S(thioether)-ligated Cu(II)-superoxo with enhanced reactivity.
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[1] K. Karlin,et al. Mechanistic Insights into the Oxidation of Substituted Phenols via Hydrogen Atom Abstraction by a Cupric–Superoxo Complex , 2014, Journal of the American Chemical Society.
[2] A. R. McDonald,et al. Nucleophilic reactivity of a copper(II)-superoxide complex. , 2014, Angewandte Chemie.
[3] K. Karlin,et al. Tuning of the Copper–Thioether Bond in Tetradentate N3S(thioether) Ligands; O–O Bond Reductive Cleavage via a [CuII2(μ-1,2-peroxo)]2+/[CuIII2(μ-oxo)2]2+ Equilibrium , 2014, Journal of the American Chemical Society.
[4] K. Karlin,et al. Observation of a Cu(II)(2) (μ-1,2-peroxo)/Cu(III)(2) (μ-oxo)(2) equilibrium and its implications for copper-dioxygen reactivity. , 2014, Angewandte Chemie.
[5] Li Tian,et al. Copper active sites in biology. , 2014, Chemical reviews.
[6] Judith B. Rommel,et al. Reaction Mechanism of the Bicopper Enzyme Peptidylglycine α-Hydroxylating Monooxygenase* , 2014, The Journal of Biological Chemistry.
[7] Kaoru Mieda,et al. A copper complex supported by an N2S-tridentate ligand inducing efficient heterolytic O-O bond cleavage of alkylhydroperoxide. , 2014, Dalton transactions.
[8] K. Karlin,et al. Correlation of the electronic and geometric structures in mononuclear copper(II) superoxide complexes. , 2013, Inorganic chemistry.
[9] G. Henkel,et al. An Approach to Model the Active Site of Peptidglycine‐α‐hydroxylating monooxygenase (PHM) , 2013 .
[10] Paulina R. Martínez-Alanis,et al. Copper versus thioether-centered oxidation: mechanistic insights into the non-innocent redox behavior of tripodal benzimidazolylaminothioether ligands. , 2013, Chemistry.
[11] K. Karlin,et al. Cupric superoxo-mediated intermolecular C-H activation chemistry. , 2011, Journal of the American Chemical Society.
[12] C. Cramer,et al. An anionic, tetragonal copper(II) superoxide complex. , 2010, Journal of the American Chemical Society.
[13] K. Karlin,et al. Sulfur donor atom effects on copper(I)/O(2) chemistry with thioanisole containing tetradentate N(3)S ligand leading to μ-1,2-peroxo-dicopper(II) species. , 2010, Inorganic chemistry.
[14] K. Karlin,et al. Thioether S-ligation in a side-on micro-eta2:eta2-peroxodicopperii complex. , 2010, Chemical communications.
[15] K. Karlin,et al. Toluene and ethylbenzene aliphatic C-H bond oxidations initiated by a dicopper(II)-mu-1,2-peroxo complex. , 2009, Journal of the American Chemical Society.
[16] M. Kubo,et al. Mononuclear copper(II)-superoxo complexes that mimic the structure and reactivity of the active centers of PHM and DbetaM. , 2009, Journal of the American Chemical Society.
[17] K. Nicholas,et al. Imidazole substituent effects on oxidative reactivity of tripodal(imid)2(thioether)CuI complexes. , 2008, Inorganic chemistry.
[18] K. Karlin,et al. A 1:1 copper-dioxygen adduct is an end-on bound superoxo copper(II) complex which undergoes oxygenation reactions with phenols. , 2007, Journal of the American Chemical Society.
[19] K. Hodgson,et al. Dioxygen reactivity of a copper(I) complex with a N3S thioether chelate; peroxo-dicopper(II) formation including sulfur-ligation. , 2006, Inorganic chemistry.
[20] A. Roitberg,et al. The catalytic mechanism of peptidylglycine alpha-hydroxylating monooxygenase investigated by computer simulation. , 2006, Journal of the American Chemical Society.
[21] Klaus Harms,et al. Crystallographic characterization of a synthetic 1:1 end-on copper dioxygen adduct complex. , 2006, Angewandte Chemie.
[22] C. Cramer,et al. Effects of thioether substituents on the O2 reactivity of beta-diketiminate-Cu(I) complexes: probing the role of the methionine ligand in copper monooxygenases. , 2006, Journal of the American Chemical Society.
[23] K. Yoshizawa,et al. Catalytic mechanism of dopamine β-monooxygenase mediated by Cu(III)-oxo , 2006 .
[24] J. Klinman. The Copper-Enzyme Family of Dopamine β-Monooxygenase and Peptidylglycine α-Hydroxylating Monooxygenase: Resolving the Chemical Pathway for Substrate Hydroxylation* , 2006, Journal of Biological Chemistry.
[25] K. Karlin,et al. Oxidant types in copper–dioxygen chemistry: the ligand coordination defines the Cun-O2 structure and subsequent reactivity , 2004, JBIC Journal of Biological Inorganic Chemistry.
[26] B. Eipper,et al. Oxygen activation by the noncoupled binuclear copper site in peptidylglycine alpha-hydroxylating monooxygenase. Spectroscopic definition of the resting sites and the putative CuIIM-OOH intermediate. , 2004, Biochemistry.
[27] S. Prigge,et al. Dioxygen Binds End-On to Mononuclear Copper in a Precatalytic Enzyme Complex , 2004, Science.
[28] E. Solomon,et al. Oxygen activation by the noncoupled binuclear copper site in peptidylglycine alpha-hydroxylating monooxygenase. Reaction mechanism and role of the noncoupled nature of the active site. , 2004, Journal of the American Chemical Society.
[29] T. D. Stack,et al. Structure and spectroscopy of copper-dioxygen complexes. , 2004, Chemical reviews.
[30] K. Karlin,et al. Copper(I)-dioxygen reactivity of [(L)Cu(I)](+) (L = tris(2-pyridylmethyl)amine): kinetic/thermodynamic and spectroscopic studies concerning the formation of Cu-O2 and Cu2-O2 adducts as a function of solvent medium and 4-pyridyl ligand substituent variations. , 2003, Inorganic chemistry.
[31] S. Hirota,et al. Hydroperoxo--copper(II) complex stabilized by N(S)s-type ligand having a phenyl thioether. , 2001, Journal of the American Chemical Society.
[32] J. Klinman. Mechanisms Whereby Mononuclear Copper Proteins Functionalize Organic Substrates. , 1996, Chemical reviews.
[33] Y. Moro-oka,et al. A Monomeric Side-On Superoxocopper(II) Complex: Cu(O2)(HB(3-tBu-5-iPrpz)3) , 1994 .
[34] R. Drago,et al. Hydrogen-bonding interactions involving metal-bound dioxygen , 1980 .