STRUCTURAL STUDIES OF BACTERIAL MULTICOMPONENT MONOOXYGENASES

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 细菌多组分单加氧酶(BMMS)，如甲烷单加氧酶(MMO)、甲苯/邻二甲苯单加氧酶(TOMO)和苯酚羟基酶(PH)等，催化饱和烃和芳香烃的区域和对映选择性氧化生成醇、酚、儿茶酚和环氧化物。在BMM羟基酶中，需要调节和还原酶蛋白质组分来实现催化作用，BMM羟基酶含有羧酸桥联的非血红素二铁活性部位，氧化反应发生在氧激活的中间体上。寻找MMO羟基酶与调节蛋白MMOB和相关抑制蛋白MMOD的复合体以及MMOH-O2中间体的结构，以探索MMO系统中各组分的相互作用和反应途径。成分蛋白质复合体、含氧中间体和二铁(II)还原、金属重组和突变形式的TOMO和PH羟基酶及其复合体的结构也将同样被追寻。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Bacterial Multicomponent Monooxygenases (BMMs) such as methane monooxygenase (MMO), toluene/o-xylene monooxygenase (ToMO), and phenol hydroxylase (PH) catalyze the regio- and enantioselective oxidation of saturated and aromatic hydrocarbons to yield alcohols, phenols, catechols, and epoxides. Regulatory and reductase protein components are required to effect catalysis in BMM hydroxylases, which contain carboxylate-bridged non-heme diiron active sites where the oxidation reactions occur at a dioxygen-activated intermediate. Structures of the MMO hydroxylase in complex with the regulatory protein MMOB and the related inhibitory protein MMOD, together with MMOH-O2 intermediates, are sought to probe component interactions and reactive pathways in the MMO system. Structures of component protein complexes, oxygenated intermediates, and the diiron(II) reduced, metal-reconstituted, and mutant forms of ToMO and PH hydroxylases and their complexes will similarly be pursued.