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EC Number Cofactor Commentary Reference
Display the reaction diagram Show all sequences 2.8.4.3S-adenosyl-L-methionine the enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes 725354
Display the reaction diagram Show all sequences 2.8.4.3[4Fe-4S]-center enzyme MiaB contains both iron and sulfide and an apoprotein form can chelate as much as 2.5-3 iron and 3-3.5 sulfur atoms per polypeptide chain. Under reducing and anaerobic conditions, a [4Fe-4S] cluster is present, whereas [2Fe-2S] and [3Fe-4S] forms are generated under aerobic conditions. Residues Cys157, Cys161, and Cys164 are involved in iron chelation, and the cluster is essential for activity 727836
Display the reaction diagram Show all sequences 2.8.4.3[4Fe-4S]-center presence of two distinct [4Fe-4S]2+,1+ clusters in the protein. One is coordinated by residues Cys150, Cys154, and Cys157 in the radical-AdoMet motif, and the other is proposed to be coordinated by the three N-terminal conserved cysteines Cys10, Cys46, and Cys79. The two [4Fe-4S]2+ clusters have similar UV-visible absorption, resonance Raman, and Moessbauer properties but differ in terms of redox properties and the EPR properties of the reduced [4Fe-4S]1+ clusters 726947
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