title: Heme A biosynthesis.
abstract: Respiration in plants, most animals and many aerobic microbes is dependent on heme A. This is a highly specialized type of heme found as prosthetic group in cytochrome a-containing respiratory oxidases. Heme A differs structurally from heme B (protoheme IX) by the presence of a hydroxyethylfarnesyl group instead of a vinyl side group at the C2 position and a formyl group instead of a methyl side group at position C8 of the porphyrin macrocycle. Heme A synthase catalyzes the formation of the formyl side group and is a poorly understood heme-containing membrane bound atypical monooxygenase. This review presents our current understanding of heme A synthesis at the molecular level in mitochondria and aerobic bacteria. This article is part of a Special Issue entitled: Biogenesis/Assembly of Respiratory Enzyme Complexes.
authors.affiliation: Microbiology Group, Department of Biology, Lund University, Sweden. Lars.Hederstedt@biol.lu.se
authors.forename: Lars
authors.initials: L
authors.lastname: Hederstedt
mesh_terms: D000818:Animals; D001419:Bacteria / Q000378:metabolism; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D002734:Chlorophyll / Q000096:biosynthesis; D004579:Electron Transport; D019143:Evolution, Molecular; D005294:Ferrochelatase / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D006418:Heme / Q000031:analogs & derivatives* / Q000096:biosynthesis / Q000737:chemistry / Q000502:physiology; D006801:Humans; D008928:Mitochondria / Q000201:enzymology / Q000378:metabolism; D020125:Mutation, Missense; D011487:Protein Conformation
chemical_list: D001426:Bacterial Proteins; D002734:Chlorophyll; C027728:heme a; D006418:Heme; C037184:chlorophyll b; D005294:Ferrochelatase