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Biochem Biophys Res Commun. 2002 Jul 5;295(1):182-6.

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

Author information

1
State Key Laboratory for Oxo Synthesis and Selective Oxidation, Lanzhou Institute of Chemical Physics, Chinese Academy of Sciences, Lanzhou 730000, PR China. xinjy1966@hotmail.com

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.

PMID:
12083787
DOI:
10.1016/s0006-291x(02)00647-2
[Indexed for MEDLINE]

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