1.14.17.1	copper	contains copper	728562	
1.14.17.1	Cu2+	-	438609, 438631, 438632	
1.14.17.1	Cu2+	1.1 Cu2+/subunit, increasing stimulation of activity by addition of up to 1 Cu2+/subunit, further additions up to at least 4 Cu/subunit gave neither stimulation nor inhibition	438628	
1.14.17.1	Cu2+	2,6-dimethylphenyl isocyanide as the isocyanide ligand demonstrated, first: the formation of a mono-DIMPI-four-coordinate complex at each copper, second: the formation of complexes containing more than one isocyanide per copper	438635	
1.14.17.1	Cu2+	3 mol of copper per mol of tetramer, MW 290000	438623	
1.14.17.1	Cu2+	4 atoms of tightly bound copper per tetramer	438602	
1.14.17.1	Cu2+	a copper protein	438589, 438601, 438604, 438608, 438623, 438628	
1.14.17.1	Cu2+	about 8 Cu2+ per tetramer	438601	
1.14.17.1	Cu2+	DBH is an ascorbate-dependent glycoprotein that requires two type 2 bound copper ions per subunit to be active. copper sites are labile and termed CuH and CuM, respectively. CuH is coordinated to three histidines and CuM to two histidines and a methionine. CuM is involved in dioxygen binding and is the site for substrate hydroxylation, and CuH is the site of electron transfer	746431	
1.14.17.1	Cu2+	enzyme contains a constant amount of Cu2+, 2 mol per mol of protein, and a variable amount of Cu2+, copper content is a linear function of the purity of the enzyme	438608