STRUCTURAL STUDIES OF BACTERIAL MULTICOMPONENT MONOOXYGENASES

细菌多组分单加氧酶的结构研究

• 批准号: 7597911
• 负责人: Stephen J. Lippard
• 金额: $ 0.28万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-03-01 至 2008-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7597911
• 关键词: Active Sites; Alcohols; Aromatic Hydrocarbons; Catalysis; Catechols; Complex; Computer Retrieval of Information on Scientific Projects Database; Dioxygen; Epoxy Compounds; Funding; Grant; Heme; Institution; Metals; Methane hydroxylase; Mixed Function Oxygenases; Oxidoreductase; Pathway interactions; Phenol 2-monooxygenase; Phenols; Proteins; Reaction; Research; Research Personnel; Resources; Source; Structure; System; United States National Institutes of Health; carboxylate; genetic regulatory protein; mutant; oxidation; reconstitution; toluene 2-xylene monooxygenase

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.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目及 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 细菌多组分单加氧酶 (BMM)，例如甲烷单加氧酶 (MMO)、甲苯/邻二甲苯单加氧酶 (ToMO) 和苯酚羟化酶 (PH)，可催化饱和烃和芳香烃的区域选择性和对映选择性氧化，生成醇、酚、儿茶酚、和环氧化物。 BMM 羟化酶的催化作用需要调节蛋白和还原酶蛋白成分，该酶含有羧酸桥联的非血红素二铁活性位点，其中氧化反应发生在双氧激活的中间体处。 MMO 羟化酶与调节蛋白 MMOB 和相关抑制蛋白 MMOD 的复合物以及 MMOH-O2 中间体的结构，旨在探测 MMO 系统中的成分相互作用和反应途径。组分蛋白复合物、含氧中间体以及二铁 (II) 还原、金属重构和 ToMO 和 PH 羟化酶及其复合物的突变形式的结构也将类似地进行研究。