1.14.18.3	bacteriohemerythrin	enhances enzyme activity. The maximum activity is observed at a enzyme to bacteriohemerythrin concentration ratio of 4:1	728079	
1.14.18.3	catalase	increases pMMO activity, catalyzes decomposition of H2O2, on pMMO activity	705192	
1.14.18.3	Cu2+	pMMO, optimal at 0.3 mM	438944	
1.14.18.3	Fe3+	pMMO, optimal at 5.0 mM	438944	
1.14.18.3	lauryl maltoside	the stimulatory effect of lauryl maltoside is responsible for the initial increase in duroquinol-dependent activity of the pellet, but no activity with NADH is observed after this solubilization	713934	
1.14.18.3	methanobactin-Cu2+ complex	stimulation by methanobactin-Cu2+ complex, no activation in absence of copper, methanobactin is isolated from Methylosinus trichosporium strain OB3b	675831	
1.14.18.3	additional information	no pMMO acivity is observed in the detergent-solubilized fraction in the presence of dithionite, ascorbate, or methyl viologen. No pMMO activity with duroquinol or NADH is observed after solubilization with Triton X-100, Tween 20, zwittergent 3-12, Nonidet-P40, or synperonic	713934	
1.14.18.3	additional information	pMMO with the full complement of copper ions does not require methanobactin for activity	684114	
1.14.18.3	additional information	the active center of pMH is located in the beta-subunit	702501	
1.14.18.3	NDH-2	type 2 NADH:quinone oxidoreductase (NDH-2) is required for activity with reductants NADH or quinol as cofactors, overview	745389