Theoretical exploration of the oxidative properties of a [(tren Me1)CuO2]+ adduct relevant to copper monooxygenase enzymes: insights into competitive dehydrogenation versus hydroxylation reaction pathways.
Singlet and triplet H-transfer reaction paths from C-H and N-H bonds were examined by means of DFT and spin-flip TD-DFT computations on the [(tren Me1)CuO2]+ adduct. The singlet energy surfaces allow its evolution towards H2O2 and an imine species. Whereas N-H cleavage appears to be a radical process, C-H rupture results in a carbocation intermediate stabilized by an adjacent N atom and an electrostatic interaction with the [CuIOOH] metal core. Upon injection of an additional electron, the latter species straightforwardly forms a hydroxylated product. Based on these computational results, a new mechanistic description of the reactivity of copper monooxygenases is proposed.
de la Lande
Aurélien
A
Laboratoire de Chimie Théorique, CNRS UMR 7616, UPMC-Univ-Paris 6, Case courrier 137, 4, place Jussieu, 75252, Paris Cedex 05, France.
Parisel
Olivier
O
Gérard
Hélène
H
Moliner
Vicente
V
Reinaud
Olivia
O
D002244:Carbon / Q000737:chemistry; D003300:Copper / Q000378:metabolism*; D004583:Electrons; D006859:Hydrogen / Q000737:chemistry*; D006861:Hydrogen Peroxide / Q000737:chemistry; D006900:Hydroxylation; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000378:metabolism; D009584:Nitrogen / Q000737:chemistry; D009942:Organometallic Compounds / Q000737:chemistry* / Q000378:metabolism; D010084:Oxidation-Reduction; D011789:Quantum Theory
C531394:(bis(aminoethyl)(methylaminoethyl)ammine)copper(I); D009942:Organometallic Compounds; D002244:Carbon; D003300:Copper; D006859:Hydrogen; D006861:Hydrogen Peroxide; D006899:Mixed Function Oxygenases; D009584:Nitrogen