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Improvements to the purification of the membrane-associated methane monooxygenase (pMMO) have resulted in preparations of pMMO with activities more representative of physiological rates, i.e., > 130 nmol•min•mg protein. Altered culture and assay conditions, optimization of detergent to protein ratio, and simplification of the purification procedure were responsible for the higher activity preparations. Changes in the culture conditions focused on the rate of copper addition. To document the physiological events that occur during copper additions, cultures were initiated in media with cells expressing soluble methane monooxygenase (sMMO), then monitored for morphological changes, copper acquisition, fatty acid concentration, as well as pMMO and sMMO expression as the copper concentration was increased from 0 1 Journal of Bacteriology (2003) 185, 5755-5764. Copyright 2003 American Society for Microbiology.

Methanobactin and the membrane-associated methane monooxygenase in methanotrophy: a tale of two proteins