2.8.1.6	FAD	enhances activity	645589	
2.8.1.6	Fe-S center	the active site of the enzyme involves a [4Fe-4S] cluster	725646	
2.8.1.6	Fe-S center	the enzyme contains a [2Fe-2S]2+ cluster	725208	
2.8.1.6	Fe-S center	the enzyme contains one [4Fe-4S]2+ cluster and one air-stable [2Fe-2S]2+ cluster per monomer	724449	
2.8.1.6	Ferredoxin	required	645585	
2.8.1.6	flavodoxin	required	645585, 645593, 645595	
2.8.1.6	iron-sulfur centre	-	702042, 702256, 702281, 704715	
2.8.1.6	additional information	not: pyridoxal 5’-phosphate	661114	
2.8.1.6	NADH	-	645611	
2.8.1.6	NADH	enhances activity	645589	
2.8.1.6	NADH	required	645610	
2.8.1.6	NADPH	-	645582, 645588, 645605, 645611	
2.8.1.6	NADPH	enhances activity	645589, 645593	
2.8.1.6	NADPH	omission results in a 100fold decrease in activity	645595	
2.8.1.6	NADPH	required	645605, 645610	
2.8.1.6	S-adenosyl-L-methionine	-	702042, 702256, 702281, 704715	
2.8.1.6	thiamine diphosphate	required	645585	
2.8.1.6	[2Fe-2S]-center	a reaction intermediate includes Arg260 as a deprotonated guanidino group, coordinated to the ferrous iron of the auxiliary [2Fe-2S] cluster as a monodentate ligand. The 9-mercaptodethiobiotin C9 is covalently coordinated to the auxiliary [2Fe-2S] cluster, which maintains the geometric and electronic structure characteristics of a typical reduced [2Fe-2S]+ cluster, with most of the spin density localized on the cluster and only a small positive spin density residing on the 9-mercaptodethiobiotin ligand via through-bond (C9 and my-thiolate) spin delocalization. C6, the target of the second hydrogen-atom abstraction, is now located in close proximity to the newly acquired thiolate sulfur	761350