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  • protein
  • During the detection of diatomic gases, the binding of the gas ligand to the heme iron induces conformational changes in the surrounding protein. (wikipedia.org)
  • Hemoproteins achieve their remarkable functional diversity by modifying the environment of the heme macrocycle within the protein matrix. (wikipedia.org)
  • Heme l is the derivative of heme B which is covalently attached to the protein of lactoperoxidase, eosinophil peroxidase, and thyroid peroxidase. (wikipedia.org)
  • myoglobin
  • In particular, heme b plays a key role as the oxygen carrier in hemoglobin in red blood cells and myoglobin in muscle cells. (wikipedia.org)
  • 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. (wikipedia.org)
  • Hemoglobin
  • In immature red blood cells, heme is the featured component of hemoglobin. (encyclopedia.com)
  • Most commonly recognized as a fundamental component of hemoglobin-the red pigment in blood responsible for the transportation of oxygen-heme also provides some of the essential nutrition that bacteria require to grow within a host. (labroots.com)
  • mitochondrial
  • Heme increases the mitochondrial activity thereby helping in activation of respiratory system Krebs Cycle and Electron Transport Chain leading to formation of adenosine triphosphate (ATP) for adequate supply of energy to the body. (wikipedia.org)
  • 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). (wikipedia.org)
  • peroxidase
  • plant peroxidases incorporate heme B. Lactoperoxidase and eosinophil peroxidase are protective enzymes responsible for the destruction of invading bacteria and virus. (wikipedia.org)
  • ligand
  • 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. (wikipedia.org)
  • liver
  • Heme is produced in several tissues in the body, but its primary biosynthesis sites are the liver and the bone marrow . (encyclopedia.com)
  • Although production is concentrated in the liver and bone marrow, heme is utilized in various capacities in virtually every tissue in the body. (encyclopedia.com)
  • histidine residue
  • A highly conserved histidine residue (His183 in B. subtilis, His263 in humans) is essential for determining the type of distortion, as well as acting as the initial proton acceptor from protoporphyrin. (wikipedia.org)
  • a histidine residue, located adjacent to the heme group, becomes positively charged under acidic conditions (which are caused by dissolved CO2 in working muscles, etc.), releasing oxygen from the heme group. (wikipedia.org)
  • chelatases
  • In the case of ferrochelatases, the reaction that chelatases catalyze is: Fe2+ + H2P → FeP + 2 H+ In the above equation H2P represents a sirohydrochlorin or a porphyrin, such as protoporphyrin IX. (wikipedia.org)
  • oxygen
  • In most cells, heme is a key building block in the construction of factors that oversee metabolism and transport of oxygen and energy. (encyclopedia.com)
  • organisms
  • Despite the wide range of organisms that synthesize protoporphyrin IX the process is largely conserved from bacteria to mammals with a few distinct exceptions in higher plants. (wikipedia.org)
  • propionic acid
  • 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. (wikipedia.org)
  • catalysis
  • The distance of heme from the PLP binding site suggests its non-role in catalysis, however deletion of the heme domain causes loss of redox sensitivity, therefore it is hypothesized that heme is a redox sensor. (wikipedia.org)
  • Therefore
  • Therefore, it is possible that CBS in slime molds and insects are hemeproteins that suggest that the heme domain is an early evolutionary innovation that arose before the separation of animals and the slime molds. (wikipedia.org)
  • biosynthetic pathway
  • Coproporphyrinuria can be caused by other stressors to the heme biosynthetic pathway, such as liver disease, lead poisoning and certain bone marrow disorders. (wikipedia.org)
  • The following genes encode enzymes that catalyze the various steps in the heme biosynthetic pathway: ALAD: aminolevulinate, delta-, dehydratase ALAS1: aminolevulinate, delta-, synthase 1 ALAS2: aminolevulinate, delta-, synthase 2 (sideroblastic/hypochromic anemia) CPOX: coproporphyrinogen oxidase FECH: ferrochelatase (protoporphyria) HMBS: hydroxymethylbilane synthase PPOX: protoporphyrinogen oxidase UROD: uroporphyrinogen decarboxylase UROS: uroporphyrinogen III synthase (congenital erythropoietic porphyria) Variegate porphyria is caused by mutations in the PPOX gene. (wikipedia.org)
  • residues
  • For example, the ability of hemoglobin to effectively deliver oxygen to tissues is due to specific amino acid residues located near the heme molecule. (wikipedia.org)
  • 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. (wikipedia.org)
  • D. melanogaster and D. discoides have truncated N-terminal extensions and therefore prevent the conserved histidine and cysteine heme ligand residues. (wikipedia.org)
  • Eosinophil peroxidase is a heme peroxidase, its activities including the oxidation of halide ions to bacteriocidal reactive oxygen species, the cationic disruption of bacterial cell walls, and the post-translational modification of protein amino acid residues. (wikipedia.org)
  • The hydrophobic lips, consisting of the highly conserved residues 300-311, face the inner mitochondrial membrane and facilitate the passage of the poorly soluble protoporphyrin IX substrate and the heme product via the membrane. (wikipedia.org)
  • mitochondrial
  • Heme-containing component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is part of the mitochondrial respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (string-db.org)
  • 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). (wikipedia.org)
  • Heme increases the mitochondrial activity thereby helping in activation of respiratory system Krebs Cycle and Electron Transport Chain leading to formation of adenosine triphosphate (ATP) for adequate supply of energy to the body. (wikipedia.org)
  • hemoglobin
  • BIOSYNTHESIS OF HEMOGLOBIN TABLE II% Uptake Few Experiment A Experiment B Control 29 52 Dialyzed (INTO) 9 16 Reconstituted 27 Glutathione ( 1 ~ 10 - 3M) 19 Glutathione ( 1 x 10 ~M) 52REFERENCES1~ Goldberg, A., Ashenbrucker, H., Cartwright, G. E., and Wintrobe, M. M.: Studieson the biosynthesis of heme in vitro by Adrian erythrocytes, Blood 11: 821, 1957.2. (spaceshipsla.com)
  • 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. (wikipedia.org)
  • In particular, heme b plays a key role as the oxygen carrier in hemoglobin in red blood cells and myoglobin in muscle cells. (wikipedia.org)
  • hemoproteins
  • 1,2 Human COX-1 and COX-2 are two structurally homologous hemoproteins responsible for the biosynthesis of prostaglandin H 2 from arachidonic acid (AA). (rsc.org)
  • accumulate
  • The process is tightly controlled so that cells produce the amount of heme needed and do not accumulate too much of the heme precursor. (spaceshipsla.com)
  • The cells of LTS3 mutants accumulate in darkness the MgCh substrate, protoporphyrin IX, and produce orange colonies greening in the light. (deepdyve.com)
  • The combination of this increased demand and reduced activity of uroporphyrinogen decarboxylase disrupts heme production and allows byproducts of the process to accumulate in the body, triggering the signs and symptoms of porphyria cutanea tarda. (wikipedia.org)
  • peroxidase
  • plant peroxidases incorporate heme B. Lactoperoxidase and eosinophil peroxidase are protective enzymes responsible for the destruction of invading bacteria and virus. (wikipedia.org)
  • Redox
  • The heme iron serves as a source or sink of electrons during electron transfer or redox chemistry. (wikipedia.org)
  • The distance of heme from the PLP binding site suggests its non-role in catalysis, however deletion of the heme domain causes loss of redox sensitivity, therefore it is hypothesized that heme is a redox sensor. (wikipedia.org)
  • histidine residue
  • a histidine residue, located adjacent to the heme group, becomes positively charged under acidic conditions (which are caused by dissolved CO2 in working muscles, etc.), releasing oxygen from the heme group. (wikipedia.org)
  • A highly conserved histidine residue (His183 in B. subtilis, His263 in humans) is essential for determining the type of distortion, as well as acting as the initial proton acceptor from protoporphyrin. (wikipedia.org)
  • iron
  • Activated NRF2 bound the antioxidant response element (ARE) in promoters of several known and novel target genes involved in iron homeostasis and heme metabolism, including known targets FTL and FTH1 , as well as novel binding in the globin locus control region. (hindawi.com)
  • Nongenetic factors such as alcohol abuse, excess iron, and others listed above can increase the demand for heme and the enzymes required to make heme. (wikipedia.org)
  • propionic acid
  • 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. (wikipedia.org)