X-RAY CRYSTALLOGRAPHIC STUDIES OF PARTICULATE METHANE MONOOXYGENASE

颗粒甲烷单加氧酶的 X 射线晶体学研究

• 批准号: 7721958
• 负责人: AMY C. ROSENZWEIG
• 金额: $ 0.02万
• 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/7721958
• 关键词: Active Sites; Bathing; Binding; Bioremediations; Chemistry; Computer Retrieval of Information on Scientific Projects Database; Copper; Data; Development; Enzymes; Funding; Generations; Grant; Hydrocarbons; Institution; Laboratories; Lead; Membrane; Membrane Proteins; Metals; Methane; Methane hydroxylase; Methanol; Methods; Methylococcus capsulatus; Methylosinus trichosporium; Particulate; Research; Research Personnel; Resources; Source; Structure; Time; United States National Institutes of Health; catalyst; cell dimension; insight; programs; research study; synchrotron radiation

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. Particulate methane monooxygenase (pMMO) is a 300 kDa membrane-bound enzyme that uses a catalytic copper-containing cluster to oxidize methane, the most inert hydrocarbon, to methanol. Characterization of the pMMO active center would provide fundamental insight into the chemistry of highly reactive species and could lead to the development of more efficient industrial catalysts or new methods for bioremediation. We recently solved the structure of pMMO from Methylococcus capsulatus (Bath), and propose experiments to identify the active site and to characterize the metal centers in detail. In addition, we have crystallized pMMO from Methylosinus trichosporium OB3b and plan to solve its structure. Because these membrane protein crystals do not diffract with a laboratory x-ray source and have large unit cell dimensions, ample time to collect diffraction data using third generation synchrotron radiation is essential to our research program.

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。子项目和 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。 颗粒甲烷单加氧酶 (pMMO) 是一种 300 kDa 的膜结合酶，它使用催化含铜簇将甲烷（最惰性的碳氢化合物）氧化为甲醇。 pMMO 活性中心的表征将为高活性物质的化学提供基础见解，并可能导致更有效的工业催化剂或生物修复新方法的开发。 我们最近解析了荚膜甲基球菌（Bath）的 pMMO 结构，并提出了鉴定活性位点和详细表征金属中心的实验。 此外，我们还从毛孢甲基红窦菌OB3b中结晶出pMMO，并计划解析其结构。 由于这些膜蛋白晶体不会通过实验室 X 射线源发生衍射，并且具有较大的晶胞尺寸，因此使用第三代同步加速器辐射收集衍射数据的充足时间对于我们的研究计划至关重要。