7.1.1.3	cytochrome	the oxidase contains cytochrome b, cytochrome o	714285	
7.1.1.3	heme	-	715509, 741988, 742754	
7.1.1.3	heme	heme b and heme o3	714139, 714169, 714308, 714331, 716311	
7.1.1.3	heme	heme b562	714131	
7.1.1.3	heme	heme d and heme b558	716735	
7.1.1.3	heme	hemes B and O	715000	
7.1.1.3	heme	low-spin heme b and high-spin heme o	714141, 715399	
7.1.1.3	heme	low-spin heme b and high-spin heme o in subunit I	715003	
7.1.1.3	heme	the enzyme contains 2 mol of heme, one or both of which are heme o	714286	
7.1.1.3	heme	the enzyme contains a hexa-coordinated low-spin heme, heme B and a penta-coordinated high-spin heme, heme O	714997	
7.1.1.3	heme	the enzyme contains a low-spin b-like heme and a high-spin 6-like heme, designated cytochromes b and o respectively	714885	
7.1.1.3	heme	the enzyme contains the low spin hexacoordinate heme b558 and the high spin pentacoordinate hemes b595 and d	741957	
7.1.1.3	heme	the enzyme contains two b- and one d-type hemes as cofactors	742510	
7.1.1.3	heme	the enzyme possesses two hemes (18.1 ng/mg)	714129	
7.1.1.3	heme	the high-spin heme is magnetically coupled to a copper, CuB, forming a binuclear center which is the site of oxygen reduction to water	714132	
7.1.1.3	heme	the purified oxidase contains both protoheme and heme O	714285	
7.1.1.3	heme	the ubiquinol oxidase cytochrome b03 of Escherichia coli is a member of the respiratory heme-copper oxidase family	714135	
7.1.1.3	ubiquinol-8	-	714997, 715000	
7.1.1.3	ubiquinone-8	the bound ubiquinone at the QH site of cytochrome bo is essential for the catalytic turnover of the oxidase reactions, but it is not necessary for re-reduction of ferric heme b after the heme b-to-heme o electron transfer under flow-flash conditions	715003	
7.1.1.3	ubiquinone-8	the enzyme contains one equivalent of ubiquinone-8	714308