X-RAY CRYSTALLOGRAPHIC STUDIES OF PARTICULATE METHANE MONOOXYGENASE

该子项目是利用 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH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 中心，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（最惰性的烃）氧化为甲醇。 pMMO活性中心的表征将为高活性物种的化学性质提供基本的见解，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。 我们最近解决了从甲基球菌荚膜（浴）的pMMO的结构，并提出实验，以确定活性位点，并详细描述金属中心。 此外，我们已经从发孢甲基弯菌OB 3b中结晶出pMMO，并计划解决其结构。 由于这些膜蛋白晶体不与实验室X射线源发生反应，并且具有较大的晶胞尺寸，因此有足够的时间使用第三代同步辐射收集衍射数据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.