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

被引:517
作者
Lieberman, RL
Rosenzweig, AC
机构
[1] Northwestern Univ, Dept Biochem Mol Biol & Cell Biol, Evanston, IL 60208 USA
[2] Northwestern Univ, Dept Chem, Evanston, IL 60208 USA
基金
美国国家卫生研究院;
关键词
D O I
10.1038/nature03311
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:177 / 182
页数:6
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