来自 trichosporium 甲基孢囊菌的颗粒性甲烷单加氧酶是一种含铜酶。

Particulate methane monooxygenase from Methylosinus trichosporium is a copper-containing enzyme.

作者信息

Xin Jia-Ying, Cui Jun-Ru, Hu Xiao-Xue, Li Shu-Ben, Xia Chun-Gu, Zhu Li-Min, Wang Yi-Qun

机构信息

State Key Laboratory for Oxo Synthesis and Selective Oxidation, Lanzhou Institute of Chemical Physics, Chinese Academy of Sciences, Lanzhou 730000, PR China.

出版信息

Biochem Biophys Res Commun. 2002 Jul 5;295(1):182-6. doi: 10.1016/s0006-291x(02)00647-2.

DOI:10.1016/s0006-291x(02)00647-2

PMID:12083787

Abstract

Particulate methane monooxygenase (pMMO) has been exfoliated and isolated from membranes of the Methylosinus trichosporium IMV 3011. It appears that the stability of pMMO in the exfoliation process is increased with increasing copper concentration in the growth medium, but extensive intracytoplasmic membrane formed under higher copper concentration may inhibit the exfoliation of active pMMO from membrane. The highest total activity of purified pMMO is obtained with an initial concentration of 6 microM Cu in the growth medium. The purified MMO contains only copper and does not utilize NADH as electron donor. Treatment of purified pMMO with EDTA resulted in little change in copper level, suggesting that the copper in the pMMO is tightly bound with pMMO.

摘要

颗粒性甲烷单加氧酶（pMMO）已从甲基弯曲菌IMV 3011的细胞膜中分离出来。在剥离过程中，pMMO的稳定性似乎随着生长培养基中铜浓度的增加而提高，但在较高铜浓度下形成的大量胞内膜可能会抑制活性pMMO从膜上的剥离。当生长培养基中铜的初始浓度为6 microM时，可获得纯化pMMO的最高总活性。纯化的MMO仅含铜，不利用NADH作为电子供体。用EDTA处理纯化的pMMO后，铜含量变化不大，这表明pMMO中的铜与pMMO紧密结合。