2.8.1.6	Iron	presence of a [2Fe-2S] cluster	645582, 645583, 645588, 645600, 645604	
2.8.1.6	Iron	the 104000 Da dimeric enzyme form contains a single [2Fe-2S] cluster per dimer	645583, 645586	
2.8.1.6	Iron	the 82000 Da dimeric enzyme form contains one [2Fe-2S]cluster per monomer	645583, 645586	
2.8.1.6	Fe2+	required	645585	
2.8.1.6	FeCl3	-	645587, 645595	
2.8.1.6	FeCl3	enhances activity 3-4fold at 0.1 mM	645587	
2.8.1.6	Na2S	-	645587, 645595	
2.8.1.6	Na2S	enhances activity 3-4fold at 1 mM	645587	
2.8.1.6	Ca2+	enhances activity	645589	
2.8.1.6	Mn2+	enhances activity	645589	
2.8.1.6	Iron	1 [2Fe-2S] and 1 [4Fe-4S] cluster per monomer are essential for optimal activity	645595	
2.8.1.6	Iron	[2Fe-2S] and [4Fe-4S] cluster	645596	
2.8.1.6	Iron	[4Fe-4S] cluster	645597	
2.8.1.6	Iron	1 [2Fe-2S] per monomer, but enzyme is more active when reconstituted with an additional [4Fe-4S] cluster	645598	
2.8.1.6	Iron	in a partially purified fraction the presence of a S2- source and Fe2+ converts the predominant [2Fe-2S] into a 1:1 mixture of [2Fe-2S] and [4Fe-4S], reduced [4Fe-4S] is involved in mediating the cleavage of S-adenosylmethionine and reduced [2Fe-2S] is the sulfur source of biotin	645600	
2.8.1.6	Iron	[Fe4-S4] cluster binds S-adenosylmethionine	645602	
2.8.1.6	Fe2+	enhances activity	645589, 645605	
2.8.1.6	Iron	the enzyme contains an iron-sulfur cluster	645587, 645605, 645608, 645614	
2.8.1.6	S2-	enhances activity	645605	
2.8.1.6	Iron	[4Fe-4S] is involved in cleavage of S-adenosylmethionine	645607	
2.8.1.6	Fe2+	highly stimulates	645610	
2.8.1.6	Iron	1 [2Fe-2S] cluster per monomer, but enzyme can be reconstituted to contain an additional [4Fe-4S] cluster, both clusters must be present for tight substrate binding	645612	
2.8.1.6	FeCl3	required for formation of mixed [Fe-S] cluster state	645613	
2.8.1.6	Iron	aerobically purified enzyme contains 1.2-1.5 [2Fe-2S] clusters per monomer. Upon reduction the [Fe2-S2] clusters are converted to [Fe4-S4] clusters. The dominant stable cluster state for the enzyme is a dimer containing 2 [Fe2-S2] clusters and 2 [Fe4-S4] clusters	645613	
2.8.1.6	Na2S	required for formation of mixed [Fe-S] cluster state	645613	
2.8.1.6	FeCl3	sulfur of the iron-sulfur cluster is provided by cysteine desulfurase EC 2.8.1.7	645614, 645615	
2.8.1.6	FeCl3	binds 1 [Fe4-S4] cluster per monomer	645615	
2.8.1.6	Iron	enzyme contains two distinct Fe-S cluster binding sites, one site accomodates a (2Fe-2S)2+ cluster with partial noncysteinyl ligation, the other site accomodates a (4Fe-4S)2+ cluster that binds S-adenosyl-L-methionine and undergoes O2-induced degradation	661114	
2.8.1.6	Iron	enzyme contains a (4FE-4S) cluster that is stable during the reaction and bound to S-adenosyl-L-methionine. Additionally, enzyme contains a (2Fe-2S) cluster. About 2/3 of the (2Fe-2S) clusters are degraded by the end of a turnover experiment, degradation is initiated by reduction of the cluster	661115	
2.8.1.6	Iron	in as-prepared sample, present as (2Fe-2s)2+ cluster with incomplete cysteinyl-S coordination, reversible conversion by dithionite yields (4Fe-4S)2+, Mossbauer studies	661720	
2.8.1.6	Iron	the as-isolated form of enzyme contains an air-stable [2Fe-2S]2+ center. Enzyme can additionally accomodate an air-sensitive [4Fe-4S]2+ center which is generated by incubation under anaerobic conditions with Fe2+ and S2-. With respect to iron cluster content and characteristics, mutants N151A, H152A, N153A, D155A are similar to wild-type	672076	
2.8.1.6	Iron	[2Fe-2S]2+ cluster coordinated by C97, C128, C188 and R260. Wild-type enzyme contains 1.6 iron atoms per monomer	672097	
2.8.1.6	Iron	the [2Fe-2S]2+ cluster is implicated in the sulfur insertion step	672142	
2.8.1.6	Iron	Fe/S cluster assembly of biotin synthase strongly depends on Isu1 and Isu2 proteins	673421	
2.8.1.6	Iron	Fe/S cluster assembly on Bio2 strongly depends on the Isu1 and Isu2 proteins, Isa proteins are crucial for the in vivo function of biotin synthase but not for the de novo synthesis of its Fe/S clusters.	673421	
2.8.1.6	Iron	BioB appears to be resistant to degradation and capable of multiple turnovers only under high-iron conditions that favor repair of the FeS clusters, a process most likely mediated by the Isc or Suf iron-sulfur cluster assembly systems.	690617	
2.8.1.6	Iron	loss of the FeS clusters results in decreased thermal stability and apparent localized unfolding of BioB, particularly in the regions around Arg168 and Arg245, but not global unfolding	690617	
2.8.1.6	Iron	the [2Fe-2S]2+ cluster is both the sulfur-donating substrate and the sulfur-oxidizing cofactor	690617