4-Hydroxybutyryl-CoA dehydratase from Clostridium aminobutyricum: characterization of FAD and iron-sulfur clusters involved in an overall non-redox reaction

The catalytic mechanism of 4-hydroxybutyryl-CoA dehydratase from Clostridium aminobutyricum was determined by characterization of the FAD and iron-sulfur clusters involved in the reaction. Electron paramagnetic resonance measurements indicate transient one-electron oxidation that initiates cleavage of the beta-C-H bond. This suggests that redox reactions involving FAD and the Fe-S cluster are involved in catalysis by 4-hydroxybutyryl-CoA dehydratase.