STRUCTURAL STUDIES OF BACTERIAL MULTICOMPONENT MONOOXYGENASES

细菌多组分单加氧酶的结构研究

• 批准号: 7721732
• 负责人: Stephen J. Lippard
• 金额: $ 0.34万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-03-01 至 2009-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7721732
• 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.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 细菌多组分单加氧酶（BMM），例如甲烷单加氧酶（MMO），甲苯/o-二甲苯单加氧酶（Tomo）和苯酚羟化酶（pH）催化了饱和和芳香族性氧化的饱和和芳香氧化的氧化和芳香族氧化的含量和芳香族含量的含量和芳香族含量。需要调节和还原酶蛋白成分才能在BMM羟化酶中进行催化，后者含有羧酸桥桥的非血红素二氧活性位点，在二氧化激活的中间体处发生氧化反应。与调节蛋白MMOB和相关抑制蛋白MMOD的复合物中MMO羟化酶的结构以及MMOH-O2中间体一起探测MMO系统中的MMOH-O2中间体。组成蛋白复合物，氧化中间体以及二烷（II）的二氧化碳（II）的结构将类似地捕获Tomo和PH羟基酶的突变形式及其复合物。