Metal Complex Activation of Dioxygen

无机、生物无机和有机金属化学专业的这个项目属于生物无机化学领域。该项目的重点是模拟单加氧酶作用的非生物含金属化合物。这些酶催化氧原子从二氧结合到有机底物中，在它们的活性位点含有金属离子，主要是血红素铁、非血红素铁和铜。这些酶的反应机制尚不清楚，迄今为止还不可能用非生物试剂复制它们的反应性。为了努力发展与单加氧酶的“反应类比”，正在研究金属卟啉过氧络合物的反应，以了解更多关于O-O键切割步骤在血红素酶中的作用。为了模拟非血红素酶的作用，其中对活性部位金属的环境知之甚少，金属介导的氧原子从单氧原子供体碘基苯转移到有机底物的研究正在进行中。还在研究铁介导的氧化反应，使用含有完整O-O键的试剂，即双氧、超氧和过氧化物。这项研究的结果将为评估生物系统中的双氧活化机制和设计实验室和工业应用中的氧化反应催化剂提供有用的信息。

This project in the Inorganic, Bioinorganic and Organometallic Chemistry Program is in the area of bioinorganic chemistry. The focus of the project is nonbiological metal-containing compounds which mimick the action of monooxygenase enzymes. These enzymes, which catalyze the incorporation of oxygen atoms from dioxygen into organic substrates, contain metal ions at their active sites, principally heme iron, non-heme iron and copper. The mechanisms of the reactions of these enzymes are not understood, and it has not been possible thus far to duplicate their reactivities with nonbiological reagents. In an effort to develop "reaction analogies" to the monooxygenase enzymes, reactions of metalloporphyrin peroxo complexes are being studied to learn more about the role of the O-O bond cleavage step in the heme enzymes. To mimick the action of non-heme enzymes, where much less is known about the environment of the metal at the active site, metal-mediated oxygen atom transfer from the single oxygen atom donor iodosylbenzene to organic substrates is under investigation. Also under study are iron-mediated oxygenation reactions using reagents containing intact O-O bonds, i.e. dioxygen, superoxide and peroxide. The results of this research will provide information useful in assessing mechanisms of dioxygen activation in biological systems and in designing catalysts for oxygenation reactions for use in the laboratory and in industrial applications.