In hemoglobin an iron(II) ion is complexed by a macrocyclic porphyrin ring. The heme moiety consists of a porphyrin ring called Fe(II)-protoporphyrin IX (FP). Deficiency in the enzymes of the porphyrin pathway leads to insufficient production of heme. ALA a key precursor in the biosynthesis of the naturally occurring porphyrin, haem. It is formed by oxidative cleavage of a porphyrin in heme, which affords biliverdin. Such chelating agents include the porphyrin rings in hemoglobin and chlorophyll. Four pyrrole rings are joined in a ring structure called a porphyrin. In peroxidase reactions, the porphyrin molecule also serves as an electron source. Some of these amphiphiles are phenyl, naphthalene, phenanthrene, pyrene and porphyrin systems. The porphyrin ring is a planar dianionic, tetradentate ligand. Myoglobin contains a porphyrin ring with an iron at its center. These complexes have a high affinity for porphyrin rings which makes them effective anticancer agents. Organoiron(III) porphyrin complexes are numerous. The electronic structure of porphyrin oxoiron compounds has been reviewed. Chloroquine may be used to increase porphyrin secretion in some EPs.