EC Number   |
Metals/Ions  |
Reference |
|---|
    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 | 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 |
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 | 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 |
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 |
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 |
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 |
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 |
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 |
