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Activating Compound
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4.2.1.157
activator HadI
the activator of the 2-hydroxyisocaproyl-CoA dehydratase from Clostridium difficile is a homodimeric [4Fe-4S] cluster containing ATPase which is bound in the dimer interface. The crystal structures of the Mg-ADP, Mg-ADPNP, and nucleotide-free states of the reduced activator have been solved at 1.6-3.0 A resolution. Abstraction of the nonacidic beta-proton of the 2-hydroxyacyl-CoA compounds is achieved by the reductive generation of ketyl radicals on the substrate, which is initiated by the transfer of an electron at low redox potentials. The highly energetic electron needed on the dehydratase is donated by a [4Fe-4S] cluster containing ATPase, termed activator. ATP-hydrolysis may not be necessary for electron transfer between the activator and dehydratase. The different propensities of the ATP- versus ADP-bound activator to form a complex with the dehydratase would be in agreement with electron transfer already being enabled by binding of the ATP-bound activator to the dehydratase. ATP-hydrolysis would then be needed to regenerate the ADP-bound state of the activator whose low affinity for the dehydratase would trigger complex dissociation allowing the cycle of reduction of the activator and ATP-induced complex formation between activator and dehydratase to start again
731299
4.2.1.157
activator HadI
the homodimeric activator is extremely oxygen-sensitive. Recombinant HadI activates the dehydratase in the presence of ATP, MgCl2 and a one-electron reducing agent titanium(III) citrate or dithionite
731782
4.2.1.157
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a [4Fe-4S] cluster-containing protein activates 2-hydroxyisocaproyl-CoA dehydratase by an ATP-driven electron transfer. Reduction of the activator protein and binding of ATP induce conformational changes necessary to transfer the electron to the dehydratase. Interaction of both proteins promotes ATP hydrolysis
733599
4.2.1.157
[4Fe-4S]-center
-
733666
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