Institute of Chemistry and the Lise Meitner-Minerva Center for Computational Quantum Chemistry, The Hebrew University of Jerusalem, 91904 Jerusalem, Israel.
J Am Chem Soc. 2011 Jan 19;133(2):176-9. doi: 10.1021/ja107339h. Epub 2010 Dec 20.
This theoretical work addresses the mechanistic switch between hydroxylase (alcohol formation) and desaturase (olefin formation) activities during alkane oxidation by two non-heme high-valent oxoiron reagents, the enzyme taurine:α-ketoglutarase dioxygenase (TauD) and the synthetic shape-selective catalyst (TpOBzFe), toward cyclohexadiene, cyclohexane, cyclopentane, and ethane. As we show, the desaturase/hydroxylase steps obey unique orbital selection rules, and the mechanistic switch is determined by intrinsic reactivity factors that depend on the ligand-sphere flexibility of the oxoiron species, the substrate, and the spin states of the reaction pathways. Testable predictions are outlined.
这项理论工作研究了两种非血红素高价氧铁试剂——酶牛磺酸：α-酮戊二酸双加氧酶（TauD）和合成的选择性催化剂（TpOBzFe）在烷烃氧化过程中从羟化酶（醇形成）到去饱和酶（烯烃形成）活性的机械转换，产物为环己二烯、环己烷、环戊烷和乙烷。正如我们所表明的，去饱和酶/羟化酶步骤遵循独特的轨道选择规则，而机械转换由内在反应性因素决定，这些因素取决于氧铁物种、底物和反应途径的自旋态的配体球的灵活性。概述了可测试的预测。
