CRYSTAL-STRUCTURE OF A BACTERIAL NONHEME IRON HYDROXYLASE THAT CATALYZES THE BIOLOGICAL OXIDATION OF METHANE
CRYSTAL-STRUCTURE OF A BACTERIAL NONHEME IRON HYDROXYLASE THAT CATALYZES THE BIOLOGICAL OXIDATION OF METHANE
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DOI：
10.1038/366537a0
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发表时间：
1993-12-09
期刊：
影响因子：
64.8
通讯作者：
NORDLUND, P
中科院分区：
文献类型：
--
作者：
ROSENZWEIG, AC;FREDERICK, CA;NORDLUND, P
来自荚膜甲基球菌（Methylococcus capsulatus）（Bath）的甲烷单加氧酶的251 K α 2 β 2 γ 2二聚体羟化酶蛋白的2.2埃晶体结构揭示了催化二铁核心的几何结构。两个铁原子通过外源性氢氧化物和乙酸盐配体桥接，并进一步由四个谷氨酸残基、两个组氨酸残基和一个水分子配位。双核铁中心位于一个疏水性的活性位点空腔中，用于结合甲烷。一个延伸的峡谷在具有许多长α-螺旋的α-对之间延伸，用于催化所需的还原酶和偶联蛋白的可能对接。
The 2.2 angstrom crystal structure of the 251K alpha2beta2gamma2 dimeric hydroxylase protein of methane mono-oxygenase from Methylococcus capsulatus (Bath) reveals the geometry of the catalytic di-iron core. The two iron atoms are bridged by exogenous hydroxide and acetate ligands and further coordinated by four glutamate residues, two histidine residues and a water molecule. The dinuclear iron centre lies in a hydrophobic active-site cavity for binding methane. An extended canyon runs between alphabeta pairs, which have many long alpha-helices, for possible docking of the reductase and coupling proteins required for catalysis.