    4.1.1.81 | Fe2+ |
the wild-type MmCobD that is normoxically or anoxically purified and then reconstituted, or anoxically purified without reconstitution contains an average of 25 Fe atoms per monomer, with rather poor standard deviations . The C-terminus of MmCobD contains one or more [4Fe-4S] 2+ cluster(s). Although these [4Fe-4S]2+ cluster(s) are not required for activity, perturbations in the C-terminal domain result in the loss of Fe2+ and alterations in the enzyme activities associated with the N-terminus. The C-terminus is not required for the kinase or decarboxylase activities, the [4Fe-4S]2+ cluster-containing C-terminus may have a regulatory role, perhaps by gating the active site or facilitating the decarboxylation and or kinase reactions. Fe2+ is not detected in the N-terminus only (MmCobD1-385) protein sample |
760602 |
