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

• Published in: Biochemical and biophysical research communications Vol. 295; no. 1; pp. 182 - 186
• Main Authors: Xin, Jia-Ying, Cui, Jun-Ru, Hu, Xiao-Xue, Li, Shu-Ben, Xia, Chun-Gu, Zhu, Li-Min, Wang, Yi-Qun
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 05.07.2002
• Subjects: Activity; Chelating Agents - pharmacology; Copper; Copper - analysis; Copper - pharmacology; Dose-Response Relationship, Drug; Edetic Acid - pharmacology; EDTA; Electron donor; Exfoliation; Growth medium; Intracytoplasmic membrane; Membrane Proteins - chemistry; Membrane Proteins - isolation & purification; Membrane Proteins - metabolism; Metalloproteins - chemistry; Metalloproteins - isolation & purification; Metalloproteins - metabolism; Methane-oxidizing bacterium; Methylosinus trichosporium - drug effects; Methylosinus trichosporium - enzymology; Methylosinus trichosporium - growth & development; Oxidation-Reduction; Oxygenases - chemistry; Oxygenases - isolation & purification; Oxygenases - metabolism; Particulate methane monooxygenase; Purification; Stability; Intracytoplasmic membrane; Purification; Stability; Methane-oxidizing bacterium; Activity; Particulate methane monooxygenase; Copper; Growth medium; EDTA; Exfoliation; Electron donor

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...