Heme - wikipedia Heme Binding of oxygen to a heme prosthetic group. Heme or haem is a coordination complex `` consisting of an iron ion coordinated to a porphyrin acting as a tetradentate ligand, and to one or two axial ligands. '' The definition is loose, and many depictions omit the axial ligands. Many porphyrin - containing metalloproteins have heme as their prosthetic group ; these are known as hemoproteins. Hemes are most commonly recognized as components of hemoglobin, the red pigment in blood, but are also found in a number of other biologically important hemoproteins such as myoglobin, cytochromes, catalases, heme peroxidase, and endothelial nitric oxide synthase. The word heme is derived from Greek αἷμα haima meaning blood. Space - filling model of the Fe - protoporphyrin IX subunit of heme B. Axial ligands omitted. Color scheme : grey = iron, blue = nitrogen, black = carbon, white = hydrogen, red = oxygen. Contents 1 Function 2 Types 2.1 Major hemes 2.2 Other hemes 3 Synthesis 4 Degradation 5 In health and disease 6 Genes 7 See also 8 Notes and references Function The heme group of succinate dehydrogenase bound to histidine, an electron carrier in the mitochondrial electron transfer chain. The large semi-transparent sphere indicates the location of the iron ion. From PDB : 1YQ3 ​. Hemoproteins have diverse biological functions including the transportation of diatomic gases, chemical catalysis, diatomic gas detection, and electron transfer. The heme iron serves as a source or sink of electrons during electron transfer or redox chemistry. In peroxidase reactions, the porphyrin molecule also serves as an electron source. In the transportation or detection of diatomic gases, the gas binds to the heme iron. During the detection of diatomic gases, the binding of the gas ligand to the heme iron induces conformational changes in the surrounding protein. In general, diatomic gases only bind to the reduced heme, as ferrous Fe ( II ) while most peroxidases cycle between Fe ( III ) and Fe ( IV ) and hemeproteins involved in mitochondrial redox, oxidation - reduction, cycle between Fe ( II ) and Fe ( III ). It has been speculated that the original evolutionary function of hemoproteins was electron transfer in primitive sulfur - based photosynthesis pathways in ancestral cyanobacteria - like organisms before the appearance of molecular oxygen. Hemoproteins achieve their remarkable functional diversity by modifying the environment of the heme macrocycle within the protein matrix. For example, the ability of hemoglobin to effectively deliver oxygen to tissues is due to specific amino acid residues located near the heme molecule. Hemoglobin reversibly binds to oxygen in the lungs when the pH is high, and the carbon dioxide concentration is low. When the situation is reversed ( low pH and high carbon dioxide concentrations ), hemoglobin will release oxygen into the tissues. This phenomenon, which states that hemoglobin 's oxygen binding affinity is inversely proportional to both acidity and concentration of carbon dioxide, is known as the Bohr effect. The molecular mechanism behind this effect is the steric organization of the globin chain ; a histidine residue, located adjacent to the heme group, becomes positively charged under acidic conditions ( which are caused by dissolved CO in working muscles, etc. ), releasing oxygen from the heme group. Types Major hemes There are several biologically important kinds of heme : Heme A Heme B Heme C Heme O PubChem number 7888115 444098 444125 6323367 Chemical formula C H O N Fe C H O N Fe C H O N S Fe C H O N Fe Functional group at C -- CH ( OH ) CH Far -- CH = CH -- CH ( cystein - S - yl ) CH -- CH ( OH ) CH Far Functional group at C -- CH = CH -- CH = CH -- CH ( cystein - S - yl ) CH -- CH = CH Functional group at C -- CH =O -- CH -- CH -- CH Structure of Fe - porphyrin subunit of heme B. Structure of Fe - porphyrin subunit of heme A. Heme A is synthesized from heme B. In two sequential reactions a 17 - hydroxyethylfarnesyl moiety is added at the 2 - position and an aldehyde is added at the 8 - position. The most common type is heme B ; other important types include heme A and heme C. Isolated hemes are commonly designated by capital letters while hemes bound to proteins are designated by lower case letters. Cytochrome a refers to the heme A in specific combination with membrane protein forming a portion of cytochrome c oxidase. Other hemes The following carbon numbering system of porphyrins is an older numbering used by biochemists and not the 1 -- 24 numbering system recommended by IUPAC which is shown in the table above. Heme l is the derivative of heme B which is covalently attached to the protein of lactoperoxidase, eosinophil peroxidase, and thyroid peroxidase. The addition of peroxide with the glutamyl - 375 and aspartyl - 225 of lactoperoxidase forms ester bonds between these amino acid residues and the heme 1 - and 5 - methyl groups, respectively. Similar ester bonds with these two methyl groups are thought to form in eosinophil and thyroid peroxidases. Heme l is one important characteristic of animal peroxidases ; plant peroxidases incorporate heme B. Lactoperoxidase and eosinophil peroxidase are protective enzymes responsible for the destruction of invading bacteria and virus. Thyroid peroxidase is the enzyme catalyzing the biosynthesis of the important thyroid hormones. Because lactoperoxidase destroys invading organisms in the lungs and excrement, it is thought to be an important protective enzyme. Heme m is the derivative of heme B covalently bound at the active site of peroxide. Heme m contains the two ester bonds at the heme 1 - and 5 - methyls as in heme l found in other mammalian peroxides. In addition, a unique sulfonamides ion linkage between the sulfur of a methionyl amino - acid residue and the heme 2 - vinyl group is formed, giving this enzyme the unique capability of easily oxidizing chloride and bromide ions. Myeloperoxidase is present in mammalian neutrophils and is responsible for the destruction of invading bacteria and viruses. It also synthesizes hypobromite by `` mistake '' which is a known mutagenic compound. Heme D is another derivative of heme B, but in which the propionic acid side chain at the carbon of position 6, which is also hydroxylated, forms a γ - spirolactone. Ring III is also hydroxylated at position 5, in a conformation trans to the new lactone group. Heme D is the site for oxygen reduction to water of many types of bacteria at low oxygen tension. Heme S is related to heme B by having a formal group at position 2 in place of the 2 - vinyl group. Heme S is found in the hemoglobin of marine worms. The correct structures of heme B and heme S were first elucidated by German chemist Hans Fischer. The names of cytochromes typically ( but not always ) reflect the kinds of hemes they contain : cytochrome a contains heme A, cytochrome c contains heme C, etc. This convention may have been first introduced with the publication of the structure of heme A. Synthesis Main article : Porphyrin § Synthesis Heme synthesis in the cytoplasm and mitochondrion The enzymatic process that produces heme is properly called porphyrin synthesis, as all the intermediates are tetrapyrroles that are chemically classified as porphyrins. The process is highly conserved across biology. In humans, this pathway serves almost exclusively to form heme. In other species, it also produces similar substances such as cobalamin ( vitamin B ). The pathway is initiated by the synthesis of - aminolevulinic acid ( dALA or δALA ) from the amino acid glycine and succinyl - CoA from the citric acid cycle ( Krebs cycle ). The rate - limiting enzyme responsible for this reaction, ALA synthase, is negatively regulated by glucose and heme concentration. Mechanism of inhibition of ALAs by heme or hemin is by decreasing stability of mRNA synthesis and by decreasing the intake of mRNA in the mitochondria. This mechanism is of therapeutic importance : infusion of heme arginate or hematin and glucose can abort attacks of acute intermittent porphyria in patients with an inborn error of metabolism of this process, by reducing transcription of ALA synthase. The organs mainly involved in heme synthesis are the liver ( in which the rate of synthesis is highly variable, depending on the systemic heme pool ) and the bone marrow ( in which rate of synthesis of Heme is relatively constant and depends on the production of globin chain ), although every cell requires heme to function properly. However, due to its toxic properties, proteins such as Hemopexin ( Hx ) are required to help maintain physiological stores of iron in order for them to be used in synthesis. Heme is seen as an intermediate molecule in catabolism of hemoglobin in the process of bilirubin metabolism. Defects in various enzymes in synthesis of heme can lead to group of disorder called porphyrias, these include acute intermittent porphyria, congenital erythropoetic porphyria, porphyria cutanea tarda, hereditary coproporphyria, variegate porphyria, erythropoietic protoporphyria. Degradation Heme breakdown Degradation begins inside macrophages of the spleen, which remove old and damaged ( senescent ) erythrocytes from the circulation. In the first step, heme is converted to biliverdin by the enzyme heme oxygenase ( HMOX ). NADPH is used as the reducing agent, molecular oxygen enters the reaction, carbon monoxide ( CO ) is produced and the iron is released from the molecule as the ferrous ion ( Fe ). CO acts as a cellular messenger and functions in vasodilation. In addition, heme degradation appears to be an evolutionarily - conserved response to oxidative stress. Briefly, when cells are exposed to free radicals, there is a rapid induction of the expression of the stress - responsive heme oxygenase - 1 ( HMOX1 ) isoenzyme that catabolizes heme ( see below ). The reason why cells must increase exponentially their capability to degrade heme in response to oxidative stress remains unclear but this appears to be part of a cytoprotective response that avoids the deleterious effects of free heme. When large amounts of free heme accumulates, the heme detoxification / degradation systems get overwhelmed, enabling heme to exert its damaging effects. heme heme oxygenase - 1 biliverdin + Fe H + NADPH + O NADP + CO In the second reaction, biliverdin is converted to bilirubin by biliverdin reductase ( BVR ) : biliverdin biliverdin reductase bilirubin H + NADPH NADP Bilirubin is transported into the liver by facilitated diffusion bound to a protein ( serum albumin ), where it is conjugated with glucuronic acid to become more water - soluble. The reaction is catalyzed by the enzyme UDP - glucuronosyltransferase. bilirubin UDP - glucuronosyltransferase bilirubin diglucuronide 2 UDP - glucuronide 2 UMP + 2 P This form of bilirubin is excreted from the liver in bile. Excretion of bilirubin from liver to biliary canaliculi is an active, energy dependent and rate limiting process. The intestinal bacteria deconjugate bilirubin diglucuronide and convert bilirubin to urobilinogens. Some urobilinogen is absorbed by intestinal cells and transported into the kidneys and excreted with urine ( urobilin, which is the product of oxidation of urobilinogen, is responsible for the yellow colour of urine ). The remainder travels down the digestive tract and is converted to stercobilinogen. This is oxidized to stercobilin, which is excreted and is responsible for the color of feces. In health and disease Under homeostasis, the reactivity of heme is controlled by its insertion into the `` heme pockets '' of hemoproteins. Under oxidative stress however, some hemoproteins, e.g. hemoglobin, can release their heme prosthetic groups. The non-protein - bound ( free ) heme produced in this manner becomes highly cytotoxic, most probably due to the iron atom contained within its protoporphyrin IX ring, which can act as a Fenton 's reagent to catalyze in an unfettered manner the production of free radicals. It catalyzes the oxidation and aggregation of protein, the formation of cytotoxic lipid peroxide via lipid peroxidation and damages DNA through oxidative stress. Due to its lipophilic properties, it impairs lipid bilayers in organelles such as mitochondria and nuclei. These properties of free heme can sensitize a variety of cell types to undergo programmed cell death in response to pro-inflammatory agonists, a deleterious effect that plays an important role in the pathogenesis of certain inflammatory diseases such as malaria and sepsis. There is an association between high intake of heme iron sourced from meat and increased risk of colon cancer. The heme content of red meat is 10-fold higher than that of white meat such as chicken. Genes The following genes are part of the chemical pathway for making heme : ALAD : aminolevulinic acid, δ -, dehydratase ( deficiency causes ala - dehydratase deficiency porphyria ) ALAS1 : aminolevulinate, δ -, synthase 1 ALAS2 : aminolevulinate, δ -, synthase 2 ( deficiency causes sideroblastic / hypochromic anemia ) CPOX : coproporphyrinogen oxidase ( deficiency causes hereditary coproporphyria ) FECH : ferrochelatase ( protoporphyria ) HMBS : hydroxymethylbilane synthase ( deficiency causes acute intermittent porphyria ) PPOX : protoporphyrinogen oxidase ( deficiency causes variegate porphyria ) UROD : uroporphyrinogen decarboxylase ( deficiency causes porphyria cutanea tarda ) UROS : uroporphyrinogen III synthase ( deficiency causes congenital erythropoietic porphyria ) See also Bilirubin metabolism Chlorin Chlorophyll Cobalamin Corrin Hemin Respiration ( physiology ) Notes and references Jump up ^ https://goldbook.iupac.org/html/H/H02773.html Jump up ^ A standard biochemistry text defines heme as the `` iron - porphyrin prosthetic group of heme proteins '' ( Nelson, D.L. ; Cox, M.M. `` Lehninger, Principles of Biochemistry '' 3rd Ed. 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( 2004 ). `` Heme A Synthase Does Not Incorporate Molecular Oxygen into the Formyl Group of Heme A ''. Biochemistry. 43 ( 27 ) : 8616 -- 8624. doi : 10.1021 / bi049056m. PMID 15236569. Jump up ^ Yoshikawa, S. ( 2012 ). `` Structural studies on bovine heart cytochrome c oxidase ''. Biochim Biophys Acta. 1817 ( 4 ) : 579 -- 589. doi : 10.1016 / j. bbabio. 2011.12. 012. PMID 22236806. Jump up ^ Rae, T. ; Goff, H. ( 1998 ). `` The heme prosthetic group of lactoperoxidase. Structural characteristics of heme l and heme l - peptides ''. The Journal of Biological Chemistry. 273 ( 43 ) : 27968 -- 27977. doi : 10.1074 / jbc. 273.43. 27968. PMID 9774411. Jump up ^ Purdy, M.A. ( 1983 ). `` Effect of growth phase and cell envelope structure on susceptibility of Salmonella triumphant to the lactoperoxidase - thiocyanate - hydrogen peroxide system ''. Infect. Immun. 39 ( 3 ) : 1187 -- 95. PMC 348082. PMID 6341231. Jump up ^ Ohshima, H. 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FEBS Letters. 579 ( 21 ) : 4567 -- 70. doi : 10.1016 / j. febslet. 2005.07. 011. PMID 16087180. Jump up ^ Fischer, H. ; Orth, H. ( 1934 ). Die Chemie des Pyrrols. Liepzig : Ischemia Verlagsgesellschaft. Jump up ^ http://escholarship.umassmed.edu/gsbs_diss/121/ ^ Jump up to : Kumar, Sanjay ; Bandyopadhyay, Uday ( July 2005 ). `` Free heme toxicity and its detoxification systems in human ''. Toxicology Letters. 157 ( 3 ) : 175 -- 188. doi : 10.1016 / j. toxlet. 2005.03. 004. Jump up ^ Lehninger 's Principles of Biochemistry ( 5th ed. ). New York : W.H. Freeman and Company. 2008. p. 876. ISBN 978 - 0 - 7167 - 7108 - 1. Jump up ^ Hanafy, K.A. ( 2013 ). `` Carbon Monoxide and the brain : time to rethink the dogma ''. Curr. Pharm. Des. 19 ( 15 ) : 2771 -- 5. doi : 10.2174 / 1381612811319150013. PMC 3672861. PMID 23092321. Jump up ^ Abraham, N.G. ; Kappas, A. ( 2008 ). `` Pharmacological and clinical aspects of heme oxygenase ''. Pharmacol. 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Types of tetrapyrroles Bilanes ( Linear ) Bilirubin Biliverdin Stercobilinogen Stercobilin Urobilinogen Urobilin Phytobilins Phytochromobilin Phycobilins Phycoerythrobilin Phycocyanobilin Phycourobilin Phycoviolobilin Macrocycle Corrinoids Methylcobalamin Adenosylcobalamin Cyanocobalamin Porphyrins Protoporphyrins Protoporphyrin IX Heme ( b, c, a, o ) Zinc protoporphyrin Magnesium protoporphyrin Phytoporphyrins Chlorophyll c Protochlorophyllide Reduced porphyrins Porphyrinogens Uroporphyrinogen ( I, III ) Coproporphyrinogen ( I, III ) Protoporphyrinogen IX Chlorins Chlorophyllide ( a, b ) Chlorophyll ( a, b ) Phaeophytin ( a, b ) Bacteriochlorophyll c Bacteriochlorins Bacteriochlorophyll a Isobacteriochlorins Siroheme Sirohydrochlorin Corphins Cofactor F430 Enzyme cofactors Active forms vitamins TPP / ThDP ( B ) FMN, FAD ( B ) NAD, NADH, NADP, NADPH ( B ) Coenzyme A ( B ) PLP / P5P ( B ) Biotin ( B ) THFA / H FA, DHFA / H FA, MTHF ( B ) AdoCbl, MeCbl ( B ) Ascorbic acid ( C ) Phylloquinone ( K ), Menaquinone ( K ) Coenzyme F420 non-vitamins ATP CTP SAMe PAPS GSH Coenzyme B Cofactor F430 Coenzyme M Coenzyme Q Heme / Haem ( A, B, C, O ) Lipoic Acid Methanofuran Molybdopterin / Molybdenum cofactor PQQ THB / BH THMPT / H MPT minerals Ca Cu Fe, Fe Mg Mn Mo Ni Zn Base forms vitamins : see vitamins Retrieved from `` https://en.wikipedia.org/w/index.php?title=Heme&oldid=815920588 '' Categories : Porphyrins Biomolecules Cofactors Hidden categories : Articles containing Ancient Greek - language text All articles with unsourced statements Articles with unsourced statements from December 2016 Talk Contents About Wikipedia Bân - lâm - gú Bosanski Català Čeština Deutsch Ελληνικά Español Esperanto فارسی Français Galego Հայերեն Hrvatski Ido Bahasa Indonesia Italiano עברית Қазақша Latviešu Magyar Македонски Nederlands 日本 語 Norsk Norsk nynorsk Polski Português Română Русский Scots Simple English Slovenščina کوردی Српски / srpski Srpskohrvatski / српскохрватски Suomi Svenska Türkçe Українська Tiếng Việt 中文 Edit links This page was last edited on 18 December 2017, at 02 : 09. 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Question: to what group of organic compounds does hemoglobin belong
Answer: Heme or haem