Abstract
With the exception of Fe++, all atoms in heme are derived from succinyl-CoA and glycine. Part of heme biosynthesis occurs in mitochondria. D-ALA synthase controls the rate-limiting step in heme biosynthesis. Lead inhibits heme biosynthesis. Porphobilinogen contains the basic pyrrole ring system used to assemble other mammalian porphyrins. Some porphyrins cause photosensitization, and thus skin lesions in animals. Harderian glands secrete protoporphyrin IX. D-ALA can be used in cancer photodynamic therapy. Carbon monoxide competes with O2 for binding to the Fe++ of hemoglobin. Nitric oxide binds to hemoglobin, which may be of significance in cases of hemolysis. Fetal hemoglobin (HbF) and adult hemoglobin (HbA) do not bind 2,3-BPG with equal affinity.
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