Assembly of nonheme Mn/Fe active sites in heterodinuclear metalloproteins.

ABSTRACT: The ferritin superfamily contains several protein groups that share a common fold and metal coordinating ligands. The different groups utilize different dinuclear cofactors to perform a diverse set of reactions. Several groups use an oxygen-activating di-iron cluster, while others use di-manganese or heterodinuclear Mn/Fe cofactors. Given the similar primary ligand preferences of Mn and Fe as well as the similarities between the binding sites, the basis for metal specificity in these systems remains enigmatic. Recent data for the heterodinuclear cluster show that the protein scaffold per se is capable of discriminating between Mn and Fe and can assemble the Mn/Fe center in the absence of any potential assembly machineries or metal chaperones. Here we review the current understanding of the

SUBMITTER: Griese JJ 

PROVIDER: S-EPMC4118035 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature