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EC Number
Metals/Ions
Commentary
Reference
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
Iron
1 [2Fe-2S] per monomer, but enzyme is more active when reconstituted with an additional [4Fe-4S] cluster
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
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.; 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; the [2Fe-2S]2+ cluster is both the sulfur-donating substrate and the sulfur-oxidizing cofactor
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
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
Iron
Fe/S cluster assembly of biotin synthase strongly depends on Isu1 and Isu2 proteins; 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.
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; presence of a [2Fe-2S] cluster
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
Iron
presence of a [2Fe-2S] cluster
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