Toward delineating the structure and function of the particulate methane monooxygenase from methanotrophic bacteria.

摘要: The particulate methane monooxygenase (pMMO) is a complex membrane protein that has been difficult to isolate and purify for biochemical biophysical characterization because of its instability in detergents used solubilize the enzyme. In this perspective, we summarize progress recently made toward obtaining purified pMMO−detergent characterizing enzyme pMMO-enriched membranes. pMMO multi-copper protein, with ca. 15 copper ions sequestered into five trinuclear clusters:  two dioxygen chemistry alkane hydroxylation (catalytic or C-clusters) three provide buffer reducing equivalents re-reduce C-clusters following turnover (electron transfer E-clusters). functional when all are reduced. When under ambient aerobic conditions absence hydrocarbon substrate, only oxidized; there an apparent kinetic barrier electron from ...