1.14.13.25	copper	the enzyme expresses the soluble enzyme form under copper limitation, and the membrane-bound particulate MMO at high copper-to-biomass ratio, mechanism of the copper switch involves a tetrameric 480 kDA sensor protein MmoS, encoded by gene mmoS, as part of a two-component signaling system, domain organization, MmoS contains a FAD cofactor, indirect regulation without binding of copper to MmoS, overview	672049	
1.14.13.25	Cu2+	cells adapted to the respective medium, either lacking Cu (sMMO production) or containing 0.01 mM Cu (pMMO production)	701759	
1.14.13.25	Cu2+	component C contains no copper	438939	
1.14.13.25	Cu2+	copper genetically regulates the enzyme activity of the soluble and membrane-bound form	438928, 438929	
1.14.13.25	Cu2+	copper-containing protein component contains one copper atom per molecule	438921	
1.14.13.25	Cu2+	cytochrome component contains 0.3-0.8 atoms copper per molecule	438921	
1.14.13.25	Cu2+	expression of the genes encoding sMMO and pMMO is regulated by copper ions, with sMMO expressed solely when copper is limiting	703761	
1.14.13.25	Cu2+	metal-binding titrations of MMOD and copper	765765	
1.14.13.25	Cu2+	the membrane-bound pMMO contains 4.8 Cu2+ ions per 100 kDa protomer the purified pMMO contains 1.4 Cu2+ ions per 100 kDa protomer, the enzyme contains a dinuclear copper center	685262	
1.14.13.25	Cu2+	when allylthiourea is removed, sMMO activity is maintained for an additional 24 generations, albeit at a slightly lower level due to the presence of 0.0007 mM of Cu2+ in the feed medium	704758