Mechanisms for Methane and Ammonia Oxidation by Particulate Methane Monooxygenase

被引:1
|
作者
Siegbahn, Per E. M. [1 ]
机构
[1] Stockholm Univ, Dept Organ Chem, Arrhenius Lab, SE-10691 Stockholm, Sweden
来源
JOURNAL OF PHYSICAL CHEMISTRY B | 2024年 / 128卷 / 24期
基金
瑞典研究理事会;
关键词
CRYSTAL-STRUCTURE; BIOLOGICAL OXIDATION; MONONUCLEAR; ACTIVATION; CATALYZES;
D O I
10.1021/acs.jpcb.4c01807
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Particulate MMO (pMMO) catalyzes the oxidation of methane to methanol and also ammonia to hydroxylamine. Experimental characterization of the active site has been very difficult partly because the enzyme is membrane-bound. However, recently, there has been major progress mainly through the use of cryogenic electron microscopy (cryoEM). Electron paramagnetic resonance (EPR) and X-ray spectroscopy have also been employed. Surprisingly, the active site has only one copper. There are two histidine ligands and one asparagine ligand, and the active site is surrounded by phenyl alanines but no charged amino acids in the close surrounding. The present study is the first quantum chemical study using a model of that active site (Cu-D). Low barrier mechanisms have been found, where an important part is that there are two initial proton-coupled electron transfer steps to a bound O-2 ligand before the substrate enters. Surprisingly, this leads to large radical character for the oxygens even though they are protonated. That result is very important for the ability to accept a proton from the substrates. Methods have been used which have been thoroughly tested for redox enzyme mechanisms.
引用
收藏
页码:5840 / 5845
页数:6
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