STRUCTURAL STUDIES OF BACTERIAL MULTICOMPONENT MONOOXYGENASES

细菌多组分单加氧酶的结构研究

• 批准号: 8362193
• 负责人: Stephen J. Lippard
• 金额: $ 0.03万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-03-01 至 2012-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8362193
• 关键词: Active Sites; Alcohols; Aromatic Hydrocarbons; Biochemical; Biological; Catalysis; Catechols; Complement; Complex; Data; Dioxygen; Electron Transport; Epoxy Compounds; Funding; Grant; Hydrocarbons; Methane hydroxylase; Mixed Function Oxygenases; National Center for Research Resources; Oxidoreductase; Pathway interactions; Phenol 2-monooxygenase; Phenols; Principal Investigator; Proteins; Protons; Radiation; Research; Research Infrastructure; Resources; Source; Structure-Activity Relationship; System; United States National Institutes of Health; Xenon; carboxylate; cost; interest; mutant; oxidation; structural biology; toluene 2-xylene monooxygenase

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. 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 at which dioxygen-activated intermediates form and oxidize the hydrocarbon substrates. Crystallographic characterization of xenon-pressurized, substrate/product-soaked, and mutant forms of the ToMO hydroxylase and PH hydroxylase and hydroxylase-regulatory complex are sought to probe substrate access pathways, proton and electron transfer mechanisms, and structure-activity relationships in BMMs and diiron carboxylate protein in general. These data will complement biochemical findings on the proteins of interest and provide additional information for comparison with the MMO system in order to elucidate the mechanisms of biological hydrocarbon oxidation.

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 而子项目的主要调查员可能是由其他来源提供的， 包括其它NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 细菌多组分单加氧酶（Bacterial multiplexor monooxygenase，BMPs）如甲烷单加氧酶（methane monooxygenase，MMO）、甲苯/邻二甲苯单加氧酶（toluene/o-xylene monooxygenase，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，生成醇、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羟化酶中的催化作用，BMM羟化酶含有羧酸根桥接的非血红素二铁活性位点，在该位点处双氧活化的中间体形成并氧化烃底物。氙加压，基板/产品浸泡，和突变体形式的ToMO羟化酶和PH羟化酶和羟化酶调节复合物的晶体学表征的目的是探测基板访问途径，质子和电子转移机制，和结构-活性关系在Besides和二铁羧酸盐蛋白一般。这些数据将补充感兴趣的蛋白质的生物化学研究结果，并提供额外的信息与MMO系统进行比较，以阐明生物烃氧化的机制。