In the context of heme, metabolic biotransformation by heme oxygenase results in the selective opening of the alpha-methine bridge to form biliverdin/bilirubin. In this case, the resulting bilin carries the suffix IXα which indicates the parent molecule was protoporphyrin IX cleaved at the alpha position.
In the realm of heme metabolism, the action of heme oxygenase entails the controlled rupture of a specific bond in heme, yielding biliverdin/bilirubin. The resultant bilirubin is labeled as IXα, denoting its origin from protoporphyrin IX cleavage at the alpha site.