X-RAY CRYSTALLOGRAPHIC STUDIES OF PARTICULATE METHANE MONOOXYGENASE

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 颗粒甲烷单加氧酶(PMMO)是一种300 kDa的膜结合酶，它使用一个催化的含铜簇将甲烷氧化成甲醇，甲烷是最不活泼的碳氢化合物。对pMMO活性中心的表征将提供对高活性物种化学的基本见解，并可能导致更有效的工业催化剂的开发或生物修复的新方法。我们最近解决了从甲氧基球菌胶囊(Bath)中提取的pMMO的结构，并提出了鉴定活性中心和详细表征金属中心的实验方案。此外，我们还从天花粉霉菌OB3b中结晶出了pMMO，并计划对其结构进行解析。由于这些膜蛋白晶体不与实验室X射线源衍射，并且具有较大的单位晶胞尺寸，因此使用第三代同步辐射收集衍射数据的充足时间对我们的研究计划至关重要。

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.