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EC Number
1 [2Fe-2S] and 1 [4Fe-4S] cluster per monomer are essential for optimal activity
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
1 [2Fe-2S] per monomer, but enzyme is more active when reconstituted with an additional [4Fe-4S] cluster
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
binds 1 [Fe4-S4] cluster per monomer; sulfur of the iron-sulfur cluster is provided by cysteine desulfurase EC
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
enhances activity
enhances activity
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