2.3.1.169	CO	a cobalt-containing Co/Fe-S component of multienzyme complex serves as a methyl carrier in the pathway of methane synthesis from acetate	644678, 644854, 644857	
2.3.1.169	CO	cobalt is the active site for the methyl–transfer reaction	644864	
2.3.1.169	Co3+	part of the methylcorrinoid protein	720372	
2.3.1.169	copper	or iron, required. Copper is one of the most abundant metal species within the cells	736020	
2.3.1.169	copper	the acetyl-CoA synthase active site contains a [4Fe-4S] cluster bridged to a binuclear Cu-Ni site. Distorted Cu(I)-S3 site in the fully active enzyme in solution. Average Cu-S bond length of 2.25 A and a metal neighbor at 2.65 A, consistent with the Cu-Ni distance observed in the crystal structure. Cu-SCoA intermediate in the mechanism of acetyl-CoA synthesis. Essential and functional role for copper in the enzyme	660349	
2.3.1.169	Cu	the Ni in cluster A can be replaced by Cu yielding an inactive form of the acetyl-CoA synthase	660370	
2.3.1.169	Cu+	capture of Ni2+, Cu+ and Zn2+ by thiolate sulfurs of an N2S2Ni complex	658436	
2.3.1.169	Cu2+	the enzyme has a metallocofactor containing iron, sulfur, copper, and nickel, the cofactor responsible for the assembly of acetyl-CoA contains a [Fe4S4] cubane bridged to a copper-nickel binuclear site	644679	
2.3.1.169	Fe	a Ni/Fe-S cluster of multienzyme CO dehydrogenase/acetyl-CoA synthase complex is the active site of acetyl-CoA cleavage and synthesis	644858	
2.3.1.169	Fe	corrinoid/iron-sulfur protein required	390465, 390474, 390475, 644674, 644678, 644850, 644851, 644854, 644855, 644857, 644858, 644861, 644862, 644863