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311.
The mechanism for the oxidation of catechol by catechol oxidase has been studied using B3LYP hybrid density functional theory.
On the basis of the X-ray structure of the enzyme, the molecular system investigated includes the first-shell protein ligands
of the two metal centers as well as the second-shell ligand Cys92. The cycle starts out with the oxidized, open-shell singlet
complex with oxidation states Cu2(II,II) with a μ-η2:η2 bridging peroxide, as suggested experimentally, which is obtained from the oxidation of Cu2(I,I) by dioxygen. The substrate of each half-reaction is a catechol molecule approaching the dicopper complex: the first
half-reaction involves Cu(I) oxidation by peroxide and the second one Cu(II) reduction. The quantitative potential energy
profile of the reaction is discussed in connection with experimental data. Since no protons leave or enter the active site
during the catalytic cycle, no external base is required. Unlike the previous density functional theory study, the dicopper
complex has a charge of +2. 相似文献
312.
313.
Rufí-Salís Martí Petit-Boix Anna Villalba Gara Ercilla-Montserrat Mireia Sanjuan-Delmás David Parada Felipe Arcas Verónica Muñoz-Liesa Joan Gabarrell Xavier 《The International Journal of Life Cycle Assessment》2020,25(3):564-576
The International Journal of Life Cycle Assessment - Rooftop greenhouses (RTGs) are agricultural systems that can improve the food supply chain by producing vegetables in unused urban spaces.... 相似文献