STRUCTURAL STUDIES OF BACTERIAL MULTICOMPONENT MONOOXYGENASES

细菌多组分单加氧酶的结构研究

• 批准号: 8170154
• 负责人: Stephen J. Lippard
• 金额: $ 0.13万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-05-01 至 2011-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8170154
• 关键词: Active Sites; Alcohols; Aromatic Hydrocarbons; Biochemical; Biological; Catalysis; Catechols; Complement; Complex; Computer Retrieval of Information on Scientific Projects Database; Data; Dioxygen; Electron Transport; Epoxy Compounds; Funding; Grant; Heme; Hydrocarbons; Institution; Methane hydroxylase; Mixed Function Oxygenases; Oxidoreductase; Pathway interactions; Phenol 2-monooxygenase; Phenols; Proteins; Protons; Research; Research Personnel; Resources; Source; Structure-Activity Relationship; System; United States National Institutes of Health; Xenon; carboxylate; interest; mutant; oxidation; 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 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.

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。需要调节性和还原酶蛋白成分才能在BMM羟化酶中催化，该羟基含有羧酸盐桥接的非血红素二氧活性位点，在该位点，在该位点，二氧化物激活的中间体形成并氧化碳氢化合物底物。晶体形式的晶体形式，底物/产品浸泡以及Tomo羟化酶和pH羟化酶和羟化酶调节络合物的突变形式是为了探测底物访问途径，Proton和Electon转移机制，以及BMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMMS和含量。这些数据将补充有关感兴趣蛋白质的生化发现，并提供其他信息以与MMO系统进行比较，以阐明生物烃氧化的机制。