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.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 细菌多组分单加氧酶（Bacterial Multicomponent Monooxygenase，BMPs）如甲烷单加氧酶（Methane Monooxygenase，MMO）、甲苯/邻二甲苯单加氧酶（ToMO）和苯酚羟化酶（phenol hydroxylase，PH）催化饱和烃和芳烃的区域选择性和对映选择性氧化以产生醇、酚、儿茶酚和环氧化物。需要调节和还原酶蛋白组分来实现BMM羟化酶中的催化，BMM羟化酶含有羧酸根桥接的非血红素二铁活性位点，其中氧化反应发生在双氧活化的中间体处。MMO羟化酶与调节蛋白MMOB和相关抑制蛋白MMOD的复合物的结构，以及MMOH-O2中间体，试图探测MMO系统中的组分相互作用和反应途径。组分蛋白质复合物，含氧中间体，和二铁（II）还原，金属重组，和突变形式的ToMO和PH羟化酶及其复合物的结构将同样追求。