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Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane

机译:膜结合的金属酶的晶体结构,催化甲烷的生物氧化

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Particulate methane monooxygenase ( pMMO) is an integral membrane metalloenzyme that catalyses the conversion of methane to methanol. Knowledge of how pMMO performs this extremely challenging chemistry may have an impact on the use of methane as an alternative energy source by facilitating the development of new synthetic catalysts. We have determined the structure of pMMO from the methanotroph Methylococcus capsulatus ( Bath) to a resolution of 2.8 Angstrom. The enzyme is a trimer with an alpha(3)beta(3)gamma(3) polypeptide arrangement. Two metal centres, modelled as mononuclear copper and dinuclear copper, are located in soluble regions of each pmoB subunit, which resembles cytochrome c oxidase subunit II. A third metal centre, occupied by zinc in the crystal, is located within the membrane. The structure provides new insight into the molecular details of biological methane oxidation.
机译:颗粒甲烷单加氧酶(pMMO)是一种不可或缺的膜金属酶,可催化甲烷向甲醇的转化。关于pMMO如何执行这种极具挑战性的化学反应的知识可能会通过促进新型合成催化剂的开发,而对甲烷作为替代能源的使用产生影响。我们已经确定了从甲烷营养缺陷型甲基球菌(Bath)到2.8埃分辨率的pMMO的结构。该酶是具有alpha(3)beta(3)gamma(3)多肽排列的三聚体。建模为单核铜和双核铜的两个金属中心位于每个pmoB亚基的可溶区域,类似于细胞色素c氧化酶亚基II。膜中有第三个金属中心,被晶体中的锌占据。该结构为生物甲烷氧化的分子细节提供了新的见识。

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