Heme Oxygenase-1: A ubiquitous stress-responsive enzyme that catalyzes the oxidative cleavage of HEME to yield IRON; CARBON MONOXIDE; and BILIVERDIN.Heme Oxygenase (Decyclizing): A mixed function oxidase enzyme which during hemoglobin catabolism catalyzes the degradation of heme to ferrous iron, carbon monoxide and biliverdin in the presence of molecular oxygen and reduced NADPH. The enzyme is induced by metals, particularly cobalt. EC 1.14.99.3.Heme: The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.Hemeproteins: Proteins that contain an iron-porphyrin, or heme, prosthetic group resembling that of hemoglobin. (From Lehninger, Principles of Biochemistry, 1982, p480)Protoporphyrins: Porphyrins with four methyl, two vinyl, and two propionic acid side chains attached to the pyrrole rings. Protoporphyrin IX occurs in hemoglobin, myoglobin, and most of the cytochromes.Carbon Monoxide: Carbon monoxide (CO). A poisonous colorless, odorless, tasteless gas. It combines with hemoglobin to form carboxyhemoglobin, which has no oxygen carrying capacity. The resultant oxygen deprivation causes headache, dizziness, decreased pulse and respiratory rates, unconsciousness, and death. (From Merck Index, 11th ed)Myoglobin: A conjugated protein which is the oxygen-transporting pigment of muscle. It is made up of one globin polypeptide chain and one heme group.Porphyrins: A group of compounds containing the porphin structure, four pyrrole rings connected by methine bridges in a cyclic configuration to which a variety of side chains are attached. The nature of the side chain is indicated by a prefix, as uroporphyrin, hematoporphyrin, etc. The porphyrins, in combination with iron, form the heme component in biologically significant compounds such as hemoglobin and myoglobin.Iron: A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN.Oxidation-Reduction: A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).Spectrum Analysis, Raman: Analysis of the intensity of Raman scattering of monochromatic light as a function of frequency of the scattered light.Spectrophotometry: The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.Ferrochelatase: A mitochondrial enzyme found in a wide variety of cells and tissues. It is the final enzyme in the 8-enzyme biosynthetic pathway of HEME. Ferrochelatase catalyzes ferrous insertion into protoporphyrin IX to form protoheme or heme. Deficiency in this enzyme results in ERYTHROPOIETIC PROTOPORPHYRIA.Heptanoates: Salts and esters of the 7-carbon saturated monocarboxylic acid heptanoic acid.Metalloporphyrins: Porphyrins which are combined with a metal ion. The metal is bound equally to all four nitrogen atoms of the pyrrole rings. They possess characteristic absorption spectra which can be utilized for identification or quantitative estimation of porphyrins and porphyrin-bound compounds.Cytochrome c Group: A group of cytochromes with covalent thioether linkages between either or both of the vinyl side chains of protoheme and the protein. (Enzyme Nomenclature, 1992, p539)HemopexinHemoglobins: The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements.Electron Spin Resonance Spectroscopy: A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.Databases, Protein: Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.Internet: A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.User-Computer Interface: The portion of an interactive computer program that issues messages to and receives commands from a user.Software: Sequential operating programs and data which instruct the functioning of a digital computer.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Sequence Analysis, Protein: A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.Mixed Function Oxygenases: Widely distributed enzymes that carry out oxidation-reduction reactions in which one atom of the oxygen molecule is incorporated into the organic substrate; the other oxygen atom is reduced and combined with hydrogen ions to form water. They are also known as monooxygenases or hydroxylases. These reactions require two substrates as reductants for each of the two oxygen atoms. There are different classes of monooxygenases depending on the type of hydrogen-providing cosubstrate (COENZYMES) required in the mixed-function oxidation.Biliverdine: 1,3,6,7-Tetramethyl-4,5-dicarboxyethyl-2,8-divinylbilenone. Biosynthesized from hemoglobin as a precursor of bilirubin. Occurs in the bile of AMPHIBIANS and of birds, but not in normal human bile or serum.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Plasmodium falciparum: A species of protozoa that is the causal agent of falciparum malaria (MALARIA, FALCIPARUM). It is most prevalent in the tropics and subtropics.Malaria, Falciparum: Malaria caused by PLASMODIUM FALCIPARUM. This is the severest form of malaria and is associated with the highest levels of parasites in the blood. This disease is characterized by irregularly recurring febrile paroxysms that in extreme cases occur with acute cerebral, renal, or gastrointestinal manifestations.Chloroquine: The prototypical antimalarial agent with a mechanism that is not well understood. It has also been used to treat rheumatoid arthritis, systemic lupus erythematosus, and in the systemic therapy of amebic liver abscesses.Antimalarials: Agents used in the treatment of malaria. They are usually classified on the basis of their action against plasmodia at different stages in their life cycle in the human. (From AMA, Drug Evaluations Annual, 1992, p1585)BooksHistidine: An essential amino acid that is required for the production of HISTAMINE.Pseudomonas aeruginosa: A species of gram-negative, aerobic, rod-shaped bacteria commonly isolated from clinical specimens (wound, burn, and urinary tract infections). It is also found widely distributed in soil and water. P. aeruginosa is a major agent of nosocomial infection.Deuterium Exchange Measurement: A research technique to measure solvent exposed regions of molecules that is used to provide insight about PROTEIN CONFORMATION.Deuterium: Deuterium. The stable isotope of hydrogen. It has one neutron and one proton in the nucleus.Arylsulfonates: Organic sulfonic acid esters or salts which contain an aromatic hydrocarbon radical.Grape Seed Extract: Exudate from seeds of the grape plant Vitis vinifera, composed of oils and secondary plant metabolites (BIOFLAVONOIDS and polyphenols) credited with important medicinal properties.Trinidad and Tobago: An independent state in the Lesser Antilles in the West Indies, north of Venezuela, comprising the islands of Trinidad and Tobago. Its capital is Port of Spain. Both islands were discovered by Columbus in 1498. The Spanish, English, Dutch, and French figure in their history over four centuries. Trinidad and Tobago united in 1898 and were made part of the British colony of Trinidad and Tobago in 1899. The colony became an independent state in 1962. Trinidad was so named by Columbus either because he arrived on Trinity Sunday or because three mountain peaks suggested the Holy Trinity. Tobago was given the name by Columbus from the Haitian tambaku, pipe, from the natives' habit of smoking tobacco leaves. (Webster's New Geographical Dictionary, 1988, p1228, 1216 & Room, Brewer's Dictionary of Names, 1992, p555, 547)Enterocytes: Absorptive cells in the lining of the INTESTINAL MUCOSA. They are differentiated EPITHELIAL CELLS with apical MICROVILLI facing the intestinal lumen. Enterocytes are more abundant in the SMALL INTESTINE than in the LARGE INTESTINE. Their microvilli greatly increase the luminal surface area of the cell by 14- to 40 fold.Cereals: Seeds from grasses (POACEAE) which are important in the diet.Plant Proteins: Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.Estrone: An aromatized C18 steroid with a 3-hydroxyl group and a 17-ketone, a major mammalian estrogen. It is converted from ANDROSTENEDIONE directly, or from TESTOSTERONE via ESTRADIOL. In humans, it is produced primarily by the cyclic ovaries, PLACENTA, and the ADIPOSE TISSUE of men and postmenopausal women.Organic Anion Transporters, Sodium-Independent: A subclass of ORGANIC ANION TRANSPORTERS that do not rely directly or indirectly upon sodium ion gradients for the transport of organic ions.Cimetidine: A histamine congener, it competitively inhibits HISTAMINE binding to HISTAMINE H2 RECEPTORS. Cimetidine has a range of pharmacological actions. It inhibits GASTRIC ACID secretion, as well as PEPSIN and GASTRIN output.Sulfasalazine: A drug that is used in the management of inflammatory bowel diseases. Its activity is generally considered to lie in its metabolic breakdown product, 5-aminosalicylic acid (see MESALAMINE) released in the colon. (From Martindale, The Extra Pharmacopoeia, 30th ed, p907)Methotrexate: An antineoplastic antimetabolite with immunosuppressant properties. It is an inhibitor of TETRAHYDROFOLATE DEHYDROGENASE and prevents the formation of tetrahydrofolate, necessary for synthesis of thymidylate, an essential component of DNA.Taurocholic Acid: The product of conjugation of cholic acid with taurine. Its sodium salt is the chief ingredient of the bile of carnivorous animals. It acts as a detergent to solubilize fats for absorption and is itself absorbed. It is used as a cholagogue and cholerectic.Drug Resistance, Neoplasm: Resistance or diminished response of a neoplasm to an antineoplastic agent in humans, animals, or cell or tissue cultures.Kidney: Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.Cell Line, Tumor: A cell line derived from cultured tumor cells.Antineoplastic Combined Chemotherapy Protocols: The use of two or more chemicals simultaneously or sequentially in the drug therapy of neoplasms. The drugs need not be in the same dosage form.Breast Neoplasms: Tumors or cancer of the human BREAST.Receptors, Progesterone: Specific proteins found in or on cells of progesterone target tissues that specifically combine with progesterone. The cytosol progesterone-receptor complex then associates with the nucleic acids to initiate protein synthesis. There are two kinds of progesterone receptors, A and B. Both are induced by estrogen and have short half-lives.Antineoplastic Agents: Substances that inhibit or prevent the proliferation of NEOPLASMS.
  • the biological function of the group is for delivering oxygen to body tissues, such that bonding of ligand of gas molecules to the iron atom of the protein group changes the structure of the protein by amino acid group of histidine residue around the heme molecule. (wikibooks.org)
  • Heme A is a bimolecular heme that is made up of of macrocyclic ligand called a porphyrin, chelating an iron atom. (wikibooks.org)
  • Upon gaseous ligand binding, the reverse T → R allosteric transition is coupled to the iron motion toward the heme plane, and this primary motion is also considered quasi-instantaneous since the stereochemical description of Hb allostery by Perutz ( 9 , 10 ) although up to now it has never been observed. (pnas.org)
  • The first event following gaseous ligand binding , namely, the transition from domed-to-planar heme, is believed to occur in less than 0.6 ps, by analogy with the well-studied heme response to ligand release ( 11 , 12 , 24 , 25 ), although the structural constraints and energy barriers for these two opposite processes are not necessarily the same. (pnas.org)
  • Below the glass-transition temperature of the solvent, heme proteins are frozen into static conformations, and ligand rebinding is well described with a time- and temperature-independent distribution of enthalpic barriers, $g(H)$. This work addresses the relaxation of the enthalpic barriers that sets in near the glass transition of the solvent as significant protein motions occur on the time scale of rebinding. (illinois.edu)
  • Geminate rebinding from 160 to 290 K is well described in MbCO by a relaxation of all barriers by 9.3 kJ/mol without invoking any wells along the reaction coordinate representing ligand migration into the protein matrix. (illinois.edu)
  • This protein includes a natural chemoattractant peptide of 21 amino acids at the N-terminus, which is a natural ligand for formyl peptide receptor-like receptor 2 (FPRL2) and promotes calcium mobilization and chemotaxis in monocytes and dendritic cells. (creative-biogene.com)
  • Nuclear receptors E75, which regulates development in Drosophila melanogaster, and Rev-erbbeta, which regulates circadian rhythm in humans, bind heme within their ligand binding domains (LBD). (nih.gov)
  • The heme-bound ligand binding domains of E75 and Rev-erbbeta were studied using electronic absorption, MCD, resonance Raman, and EPR spectroscopies. (nih.gov)
  • Both proteins undergo redox-dependent ligand switching and CO- and NO-induced ligand displacement. (nih.gov)
  • When the heme is reduced to the Fe(II) oxidation state, the cysteine(thiolate) is replaced by a different neutral donor ligand, whose identity is not known. (nih.gov)
  • CO binds to the Fe(II) heme in both E75(LBD) and Rev-erbbeta(LBD) opposite a sixth neutral ligand, plausibly the same histidine that served as the sixth ligand in the Fe(III) state. (nih.gov)
  • Our results reveal a new function for heme as a ligand of Bach2 and as a modulatory signal involved in plasma cell differentiation. (bloodjournal.org)
  • 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)
  • 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)
  • A loss of one axial ligand or the hydrogen bonding interaction with Tyr240 resulted in an increase in the redox potential of the heme for CgHmuT to be reduced by dithionite, though the wild type was not reduced under physiological conditions. (mdpi.com)
  • This study investigates the potential of novel heme-ligand complexes, derived from heme-iron isolated from porcine hemoglobin by enzymatic hydrolysis, to use as pigments for meat products. (springer.com)
  • The ligand affinity and heme-ligand stability was assessed over time in solution by UV-Vis absorbance spectroscopy and CIELAB color space parameters. (springer.com)
  • The CIE redness score a * was used as a single measurement to propose a predictive model based on the following parameters: heme source (heme-iron extract or hemin standard), heme-to-ligand molar ratio (1:20 to 1:300), and storage time (up to 32 days). (springer.com)
  • The optimal concentration at which each ligand can be added to either heme source, as well as the stability of the red color of the formed heme-ligand complexes in-solution was determined. (springer.com)
  • No ligand showed as much affinity for heme as sodium nitrite. (springer.com)
  • Computational modeling and X-ray crystallization of the ligand binding domain (LBD) of Rev-erbs provided incentives for proposing heme as the bona fide ligand. (biomedcentral.com)
  • and the authenticity of heme as a ligand remained elusive at the time due to the lack of unified information on heme binding sites and heme-protein interaction. (biomedcentral.com)
  • Regardless of the purposes, a thorough understanding of protein-ligand interaction is essential. (biomedcentral.com)
  • Myoglobin heme free Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 11.67 kDa. (prospecbio.com)
  • The Myoglobin heme free contains N-terminal T7 tag and purified by proprietary chromatographic techniques. (prospecbio.com)
  • Myoglobin heme free although stable at 15°C for 2 weeks, should be stored at 4°C. (prospecbio.com)
  • It is proven that during cooking, as a heat-induced interaction, oxidation of myoglobin results in oxidative cleavage of porphyrin ring of heme, and some portions of heme iron are converted in to nonheme iron. (hindawi.com)
  • Ascenzi, Paolo and Coletta, Massimo and Wilson, Michael T and Fiorucci, Laura and Marino, Maria and Polticelli, Fabio and Sinibaldi, Federica and Santucci, Roberto (2015) 'Cardiolipin-cytochromeccomplex: Switching cytochromecfrom an electron-transfer shuttle to a myoglobin- and a peroxidase-like heme-protein. (essex.ac.uk)
  • A novel tyrosine-heme C−O covalent linkage in F43Y myoglobin: a new post-translational modification of heme proteins. (ebi.ac.uk)
  • Role of heme iron coordination and protein structure in the dynamics and geminate rebinding of nitric oxide to the H93G myoglobin mutant: implications for nitric oxide sensors. (mysciencework.com)
  • The influence of the heme iron coordination on nitric oxide binding dynamics was investigated for the myoglobin mutant H93G (H93G-Mb) by picosecond absorption and resonance Raman time-resolved spectroscopies. (mysciencework.com)
  • At high concentrations, (imidazole)-(NO)-6-coordinate heme is formed, and the photoinduced rebinding kinetics reveal two exponential picosecond phases ( approximately 10 and approximately 100 ps) similar to those of wild type myoglobin. (mysciencework.com)
  • We report that short-term uridine administration in C57BL/6J mice increases liver protein glycosylation profiles, reduces phosphorylation level of insulin signaling proteins, and activates the HRI-eIF-2α-ATF4 heme-deficiency stress response pathway. (nih.gov)
  • UPase1-/- mice exhibit activation of the liver HRI-eIF-2α-ATF4 heme-deficiency stress response pathway. (nih.gov)
  • Bioinformatics analysis revealed that several key metabolic pathways had changed in the absence of heme, among which glycolysis was a major pathway impaired under heme-deficient conditions. (rsc.org)
  • Protein/Protein Interactions in the Mammalian Heme Degradation Pathway" by Andrea L. M. Spencer, Ireena Bagai et al. (unl.edu)
  • Besides providing heme and its breakdown products, which are essential constituents of almost all organisms, the pathway supplies the chlorophyll (Chl) crucial for photosynthesis in cyanobacteria, algae, and plants ( Tanaka and Tanaka, 2007 ). (elifesciences.org)
  • TSPO, a stress-induced, posttranslationally regulated, early secretory pathway-localized plant cell membrane protein, belongs to the TspO/MBR family of regulatory proteins, which can bind porphyrins. (plantcell.org)
  • Mutation of the two Tyr residues in a putative ubiquitin-like ATG8 interacting motif of At-TSPO did not affect heme binding in vitro but stabilized the protein in vivo, suggesting that downregulation of At-TSPO requires an active autophagy pathway, in addition to heme. (plantcell.org)
  • Heme Deficiency Interferes with the Ras-Mitogen-activated Protein Kinase Signaling Pathway and Expression of a Subset of Neuronal Genes -- Zhu et al. (aacrjournals.org)
  • Also, other proteins which involved in the same pathway with COX10 were listed below. (creativebiomart.net)
  • A dominant theory is that there is a relative excess of specific ribosomal proteins, P53 pathway activation, and cell apoptosis ( 3 - 6 ). (sciencemag.org)
  • Based on sequence comparisons, we discuss the possibility that the protein intervenes in a kinase-dependent signal transduction pathway involved in this last function. (genetics.org)
  • In Streptococcus pyogenes , the protein SiaA (HtsA) is part of a heme uptake pathway system and involved in heme transfer from Shp to the ABC transporter. (gsu.edu)
  • In this research, two of the five proteins in the heme uptake pathway of C . diphtheriae were studied. (gsu.edu)
  • In E. coli , CcmE was found to be an intermediate in the heme delivery pathway specific for c -type cytochromes. (asm.org)
  • Here, we report on the characterization of the B. japonicum CcmE and CcmC proteins in the cytochrome c maturation pathway in a situation where they replace the corresponding E. coli orthologues. (asm.org)
  • It can also export coproporphyrin and protoporphyrin IX, which are both intermediate products in the heme biosynthetic pathway. (genecards.org)
  • Heme biosynthesis is a highly conserved pathway which is present in all kingdoms, from Archaea to higher organisms such as plants and mammals. (chalmers.se)
  • We also discuss the necessity to gain more insight into the heme biosynthesis pathway regulation, as this interacts closely with overall stress control. (chalmers.se)
  • In this work we evaluated the expression of different combinations of alpha and beta peptides and combined this with metabolic engineering of the heme biosynthetic pathway. (chalmers.se)
  • Increased sensitivity for inhibition of CYP-mediated metabolism and nitric oxide production by iNOS indicates that DPI targets heme moieties within the enzymes. (ovid.com)
  • A recombinant bacterial expression system that generates 13C-labeled heme or 15N-labeled heme in functional cytochrome P450 enzymes and other heme-containing systems is reported here using a mutant strain of Escherichia coli (HU227) in which the HemA gene is inactive. (uncg.edu)
  • Nrf2 regulates expression of genes encoding enzymes with antioxidant (e.g. heme oxygenase-1 (HO-1)) or xenobiotic detoxification (e.g. (thebiogrid.org)
  • The binding of substrates to heme enzymes has been widely assumed to occur at the so-called delta-heme edge. (le.ac.uk)
  • It is demonstrated that the genome of C. cochliodes contains genes encoding putative enzymes from all four known heme peroxidase superfamilies including bifunctional catalase-peroxidase (KatG), cytochrome c peroxidase (CcP), manganese peroxidase, two paralogs of hybrid B peroxidases (HyBpox), cyclooxygenase, linoleate diol synthase, dye-decolorizing peroxidase (DyP) of type B and three paralogs of heme thiolate peroxidases. (biomedcentral.com)
  • Interestingly, representatives from all five (super)families were found including putative bifunctional catalase-peroxidase, cytochrome c peroxidase, hybrid B peroxidases, cyclooxygenase-like enzymes, dye-decolorizing peroxidases, heme thiolate peroxidases as well as large- and small-subunit monofunctional catalases. (biomedcentral.com)
  • plant peroxidases incorporate heme B. Lactoperoxidase and eosinophil peroxidase are protective enzymes responsible for the destruction of invading bacteria and virus. (wikipedia.org)
  • Heme oxygenases are enzymes that are involved in the degradation of heme. (perkinelmer.com)
  • Consequently, the heme coordination state together with the energy barriers provided by the protein structure control the dynamics and affinity for NO-binding enzymes. (mysciencework.com)
  • The ultrafast events in the interaction of heme proteins with various gaseous ligands were studied extensively at molecular level in the last two decades by femtosecond transient absorption (TA) ( 14 , 15 ) and time-resolved IR (TR-IR) ( 16 , 17 ) spectroscopies. (pnas.org)
  • In the Fe(III) oxidation state, the nuclear receptor hemes are low spin and 6-coordinate with cysteine(thiolate) as one of the two axial heme ligands. (nih.gov)
  • Histidine in COX protein and CO or oxygen can be axial ligands. (nih.gov)
  • Space-filling model of the Fe- protoporphyrin IX subunit of heme B. Axial ligands omitted. (wikipedia.org)
  • SiaA mutants, in which alanine replaces the axial histidine (H229) and methionine (M79) ligands, as well as a lysine (K61) and cysteine (C58) located near the heme propionates, are reported. (gsu.edu)
  • The crystal structure of HmuT from Corynebacterium glutamicum (CgHmuT) reveals that heme is accommodated in the central cleft with His141 and Tyr240 as the axial ligands and that Tyr240 forms a hydrogen bond with Arg242. (mdpi.com)
  • In the continued absence of a structure of the holoform of CcmE, identification of the heme ligands is an important step in understanding the molecular function of this protein and the role of covalent heme binding to CcmE during the maturation of c-type cytochromes. (ox.ac.uk)
  • Resonance Raman spectra demonstrated that one of the heme axial ligands is a histidine residue and that the other is likely to be Tyr134. (ox.ac.uk)
  • Five alternatives to sodium nitrite were identified as possible heme ligands and stabilizing agents of the red conformation of heme. (springer.com)
  • Ahn DU, Maurer AJ (1990) Poultry meat color: kinds of heme pigments and concentrations of the ligands. (springer.com)
  • As may be seen in the figure, the left shows representations of electron-density clouds of the de-oxygenated heme group, depicted in pink, and the attached histidine residue which may be seen in light blue . (wikibooks.org)
  • We probed the heme iron motion by the evolution of the iron-histidine Raman band intensity after NO photolysis. (pnas.org)
  • The signal of diatomic binding/release can be transmitted to the overall protein structure either by in-plane/out-of-plane motion of the iron through the bound proximal histidine or by the cleavage of the iron-histidine (Fe-His) bond. (pnas.org)
  • 15 ] combined histidine affinity chromatography with a proteomics database to improve the identification of c-type heme peptides in liquid chromatography-tandem mass spectrometry experiments. (biomedcentral.com)
  • The heme group of succinate dehydrogenase bound to histidine , an electron carrier in the mitochondrial electron transfer chain . (wikipedia.org)
  • a histidine residue, located adjacent to the heme group, becomes positively charged under acidic conditions (which are caused by dissolved CO 2 in working muscles, etc.), releasing oxygen from the heme group. (wikipedia.org)
  • The heme chaperone CcmE is a novel protein that binds heme covalently via a histidine residue as part of its essential function in the process of cytochrome c biogenesis in many bacteria as well as plant mitochondria. (ox.ac.uk)
  • By expressing CcmE (CycJ) from Bradyrhizobium japonicum in E. coli we demonstrated that heme is bound covalently to this protein at a strictly conserved histidine residue. (asm.org)
  • It binds heme transiently in the periplasm at a single histidine residue and transfers it to apocytochrome c , thereby acting as a periplasmic heme chaperone ( 15 ). (asm.org)
  • In the H93G-Mb, the glycine replacing the proximal histidine does not interact with the heme iron so that exogenous substituents like imidazole may coordinate to the iron at the proximal position. (mysciencework.com)
  • In this study, we determined structural elements within PhuS that undergo conformational rearrangement on heme binding and further show that allosteric linkage between the N- and C-terminal domains of PhuS is critical for triggering heme release to HemO. (pnas.org)
  • A heme-dependent conformational rearrangement of the C-terminal domain of heme binding protein (PhuS) is required for interaction with the iron-regulated heme oxygenase (HemO). (pnas.org)
  • Herein, we further investigate the underlying mechanism of this conformational rearrangement and its implications for heme transfer via site-directed mutagenesis, resonance Raman (RR), hydrogen-deuterium exchange MS (HDX-MS) methods, and molecular dynamics (MD). HDX-MS revealed that the apo-PhuS C-terminal α6/α7/α8-helices are largely unstructured, whereas the apo-PhuS H212R variant showed an increase in structure within these regions. (pnas.org)
  • We suggest that conformational protein mobility blocks intramolecular interheme ET in bulk homogeneous solution but triggers opening of this gated ET channel in the electrochemical environment or in the membrane environment of natural respiratory cyt c(4) function. (dtu.dk)
  • Journal Article] Distal regulation of heme binding of heme oxygenase-1 mediated by conformational fluctuations. (nii.ac.jp)
  • Overall and heme environmental structures of these mutants were similar to those of the wild type, suggesting that there is little conformational change in the heme-binding cleft during heme transport reaction with binding and the dissociation of heme. (mdpi.com)
  • In most cases the proteins undergo small conformational changes upon heme binding. (biomedcentral.com)
  • Our analysis revealed that heme binding pockets show special features and that most of the heme proteins undergo small conformational changes after heme binding, suggesting the apo structures can be used for structure-based heme protein prediction and as scaffolds for future heme protein design. (biomedcentral.com)
  • Similarly to Hb ( 8 - 10 ), the signaling mechanisms are based at the molecular level on an allosteric structural change of the receptor/sensor protein coupled to a change of activity or affinity and are induced by diatomic ligation to the heme iron cofactor. (pnas.org)
  • Isotopic labeling of the heme cofactor in cytochrome p450 and other heme proteins. (uncg.edu)
  • By synthesizing several isotopomers of aminolevulinic acid with 13C or 15N at different locations, isotopes have been incorporated with high abundance into the heme cofactor of five different cytochrome P450 isoforms, along with one peroxidase. (uncg.edu)
  • In c -type cytochromes, the heme cofactor is attached covalently via two thioether bonds to a conserved CXXCH sequence motif within the apoprotein. (asm.org)
  • This cofactor is acquired from the host and is distributed and inserted into different heme-proteins such as respiratory complexes in the parasite's mitochondrion. (biochemj.org)
  • Heme A, the cofactor for all eukaryotic C c O, is synthesized via two sequential enzymatic reactions catalyzed by heme O synthase (HOS) and heme A synthase (HAS). (biochemj.org)
  • The ability to replace the native heme cofactor of proteins with an unnatural porphyrin of interest affords new opportunities to study heme protein chemistry and engineer heme proteins for new functions. (scripps.edu)
  • We further demonstrate that FLVCR mediates heme export from macrophages that ingest senescent red cells and regulates hepatic iron. (sciencemag.org)
  • In this study, we elucidated a lncRNA (UCA1)-mediated mechanism that regulates heme metabolism in human erythroid cells. (nature.com)
  • Thus, FLVCR1b regulates erythropoiesis by controlling mitochondrial heme efflux, whereas FLVCR1a expression is required to prevent hemorrhages and edema. (jci.org)
  • We show that FhtR, by managing intracellular heme concentration, regulates the functional expression of the heme-dependent catalase A (KatA), thus participating in heme detoxification. (asm.org)
  • These studies provide a first step in defining the role of protein conformation and allosteric contributions in heme transfer within bacterial heme uptake systems. (pnas.org)
  • Furthermore, the expression of genes for heme uptake changed in response to B-cell activation and heme administration. (bloodjournal.org)
  • The causative agent of diphtheriae, Corynebacterium diphtheriae , imports heme via an ABC uptake transporter. (gsu.edu)
  • Corynebacteria contain a heme uptake system encoded in hmuTUV genes, in which HmuT protein acts as a heme binding protein to transport heme to the cognate transporter HmuUV. (mdpi.com)
  • These results suggest that the heme environmental structure stabilizes the ferric heme binding in CgHmuT, which will be responsible for efficient heme uptake under aerobic conditions where Corynebacteria grow. (mdpi.com)
  • Under aerobic conditions and with lipids which bind the heme protein, the kinetics of the oxidation process as observed by the spin label method are identical to the kinetics previously observed by measurements of oxygen uptake. (scripps.edu)
  • These nuclear receptors exhibit coordination characteristics that are similar to other known redox and gas sensors, suggesting that E75 and Rev-erbbeta may function in heme-, redox-, or gas-regulated control of cellular function. (nih.gov)
  • Controlling Self-Assembly by Linking Protein Folding DNA Binding and the Redox Chemistry of Heme. (docme.ru)
  • Angewandte Chemie DNA Recognition DOI: 10.1002/ange.200463035 Controlling Self-Assembly by Linking Protein Folding, DNA Binding, and the Redox Chemistry of Heme** D. Dafydd Jones and Paul D. Barker* Biological molecules are being used extensively as selfassembling materials for the "bottom-up" creation of useful nanoscale structures with non-natural functions. (docme.ru)
  • We report kinetic data for the two-step electron transfer (ET) oxidation and reduction of the two-domain di-heme redox protein Pseudomonas stutzeri cytochrome (cyt) c(4) by [Co(bipy)(3)](2- 3-) (bipy = 2,2'-bipyridine). (dtu.dk)
  • The heme iron serves as a source or sink of electrons during electron transfer or redox chemistry. (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)
  • Like most intestinal bacteria, E. faecalis does not synthesize heme (in this report, heme refers to iron protoporphyrin IX regardless of the iron redox state). (asm.org)
  • Among such nutrients is heme, a co-factor for oxygen storage, electron transport, photosynthesis, and redox biochemistry, which is indispensable for life. (core.ac.uk)
  • BhuR contains motifs which are common to bacterial heme receptors, including a consensus FRAP domain, an NPNL domain, and two TonB boxes. (asm.org)
  • An N-terminal 32-amino-acid segment, putatively required for rhuIR -dependent regulated expression of bhuR , is present in BhuR but not in other bacterial heme receptors. (asm.org)
  • On the other hand, we had already made crystal of HmuO, a bacterial heme oxygenase, and tried to elucidate crystal structure of HmuO. (nii.ac.jp)
  • Heme inhibited the DNA binding activity of Bach2 in vitro and reduced its half-life in B cells. (bloodjournal.org)
  • When added to B-cell primary cultures, heme enhanced the transcription of Blimp-1, the master regulator of plasma cells, and skewed plasma cell differentiation toward the IgM isotype, decreasing the IgG levels in vitro. (bloodjournal.org)
  • The primary structures, optical properties, oxidative stability, and in vitro heme transfer reaction of SeShp and SeHtsA are very similar to those of S. pyogenes Shp and HtsA. (biomedcentral.com)
  • Recent studies suggest that cell surface proteins and ABC transporters are involved in heme acquisition by gram-positive bacteria ( 23 ). (asm.org)
  • The machinery involved in heme acquisition in Gram-positive bacteria is not conserved. (biomedcentral.com)
  • Difference spectra of liver microsomes, recombinant CYPs, and iNOS demonstrated that DPI altered heme-carbon monoxide interactions. (ovid.com)
  • If you cannot find the target and/or product is not available in our catalog, please click here to contact us and request the product or submit your request for custom elisa kit production , custom recombinant protein production or custom antibody production . (mybiosource.com)
  • Custom ELISA Kits, Recombinant Proteins and Antibodies can be designed, manufactured and produced according to the researcher's specifications. (mybiosource.com)
  • The feline leukemia virus, subgroup C (FeLV-C), receptor, FLVCR, is a heme export protein ( 3 ). (sciencemag.org)
  • Progesterone receptor membrane component 1 (Pgrmc1) is related to cytochrome b 5 , binds to heme, and is associated with DNA damage resistance and apoptotic suppression. (aspetjournals.org)
  • These proteins were HmuT, lipoprotein component of the ABC transporter, and HtaA, the heme receptor. (gsu.edu)
  • This effect suppressed the cellular heme-oxygenase-1 (HO-1) response and shifted macrophage iron homeostasis towards inappropriately high expression of the transferrin receptor with concurrent inhibition of ferroportin expression. (hindawi.com)
  • We are using structural and signaling studies with receptor mutants and cell/murine models to determine how kinase activity and signaling output is regulated by intermolecular interactions with the receptor C terminal tail and with cellular proteins that either adapt or suppress signals. (ucc.ie)
  • It recruits heme through HmuY, which sequesters heme from host carriers and delivers it to its cognate outer-membrane transporter, the TonB-dependent receptor HmuR. (core.ac.uk)
  • However, free heme is toxic. (sciencemag.org)
  • however, excess free heme is toxic to cells due to its lipophilic nature, lipid peroxidation capacity, and ability to catalyze the production of reactive oxygen species (reviewed in Anzaldi and Skaar, 2010 ). (frontiersin.org)
  • Through a docking study and site-directed mutagenesis, a heme-binding model for the HutZ dimer is proposed. (pubmedcentralcanada.ca)
  • Although proposed long time ago, the molecular mechanism of heme-dependent inhibition of GluTR in planta has remained elusive. (elifesciences.org)
  • Thus far, HutZ's structure and heme-binding mechanism are unknown. (pubmedcentralcanada.ca)
  • Based on the structure, the mechanism of the electron transfer from CPR to heme-HO complex accompanied with the large domain motion of CPR has been proposed. (nii.ac.jp)
  • On the basis of spectroscopic data, optical absorption and resonance Raman spectra, and enzymological analysis of HO-2 and HmuO, their heme environment and reaction mechanism were found to be identical to those of HO-1 , inducible form of mammalian heme oxygenase. (nii.ac.jp)
  • These results define a lncRNA-mediated posttranscriptional mechanism that provides a new dimension into how the fundamental heme biosynthetic process is regulated as a determinant of erythrocyte development. (nature.com)
  • Our studies are focused on determining the mechanism of action of PDLIM2 in regulating protein stability and in evaluating PDLIM2 as a biomarker for subsets of breast and other cancers. (ucc.ie)
  • The results also imply that the structure, function, and functional mechanism of the heme acquisition machinery are conserved in S. equi and S. pyogenes . (biomedcentral.com)
  • Some Gram-negative bacteria also acquire heme in a hemophore-independent mechanism. (biomedcentral.com)
  • The iron in the heme is capable of undergoing oxidation and reduction (usually to +2 and +3, though stabilized ferryl [Fe+compounds are well known in the peroxidases). (diff.org)
  • The injurious impact of free Hb has been ascribed to heme-driven oxidative processes and vascular dysfunction. (hindawi.com)
  • Oxidative heme toxicity to the blood-brain barrier has been intimately linked to some of the most severe cerebral complications of this disease [ 15 ], and efficient Hb-iron recycling is critical to support erythropoiesis during severe anemia, which is one of the major worldwide causes of malaria death [ 16 - 18 ]. (hindawi.com)
  • Heme oxygenases have been characterized as markers for oxidative stress, metabolic disorders and inflammation. (perkinelmer.com)
  • The encoded protein enhances outer and inner mitochondrial membrane permeabilization, especially under conditions of oxidative stress. (genecards.org)
  • Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. (icr.ac.uk)
  • In many cases, the product patterns of UPOs resemble those of human cytochrome P450 (P450) monooxygenases and, in fact, combine the catalytic cycle of heme peroxidases with the "peroxide shunt" of P450s. (springer.com)
  • The oxidation-state-dependent affinity of heme for protein can then be exploited to control the assembly, and conditions can be identified under which DNA binding could be controlled by electron-transfer reactions. (docme.ru)
  • A now data analysis scheme shows unequivocally that two-ET oxidation and reduction of P. stutzeri cyt c(4) is entirely dominated by intermolecular ET between the heme groups and the external reaction partner in the ms time range, with virtually no contribution from intramolecular interheme ET in this time range. (dtu.dk)
  • The results are discussed in terms of our more general understanding of substrate oxidation across other heme proteins, and the emerging role of the heme propionates at the gamma-heme edge. (le.ac.uk)
  • Evidence is presented that this loss of signal can be used as a sensitive method to study lipid oxidation catalyzed by heme proteins. (scripps.edu)
  • MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. (icr.ac.uk)
  • We investigated the ultrafast structural transitions of the heme induced by nitric oxide (NO) binding for several heme proteins by subpicosecond time-resolved resonance Raman and femtosecond transient absorption spectroscopy. (pnas.org)
  • This observed phenomenon constitutes the primary structural transition in heme proteins induced by NO binding. (pnas.org)
  • At the same time, the binding of a diatomic and subsequent T → R transition have not yet been studied by a time-resolved technique sensitive to heme structural changes. (pnas.org)
  • The rate constant dependence on the solvent viscosity has disclosed strong coupling to both a (set of) frictionally damped solvent/protein nuclear modes and intramolecular friction-less "ballistic" modes, indicative of notable protein structural mobility in the overall two-ET process. (dtu.dk)
  • This mismatch initiates more divergent structural characteristics towards their C-terminal regions, which are essential features for the heme-binding of HugZ as a heme oxygenase. (pubmedcentralcanada.ca)
  • From the comparison of crystal structures in oxidized and reduced forms, substantial amount of structural changes provoked by changing of heme iron electronic state were discovered for the first time. (nii.ac.jp)
  • The Vallone group focuses on the structural dynamics of heme proteins and work primarily with the time resolved X-ray diffraction and wide-angle x-ray scattering, spectroscopy and kinetics. (x-probe.org)
  • This research will involve training on protein engineering and crystal structural analysis. (x-probe.org)
  • The structural determination of a large number of heme proteins has made it possible to study the detailed chemical and structural properties of heme binding environment. (biomedcentral.com)
  • In this paper, we constructed a non-redundant dataset of 125 heme-binding protein chains and found that these heme proteins encompass at least 31 different structural folds with all-α class as the dominating scaffold. (biomedcentral.com)
  • To date, structure-based protein function prediction remains a major challenge in structural bioinformatics. (biomedcentral.com)
  • We analyzed the ability of B. japonicum CcmE to bind heme when it was expressed in E. coli . (asm.org)
  • The E. coli CcmE protein (CcmE Ec ) is able to bind heme in the presence of CcmABCD ( 15 ). (asm.org)
  • Both CcmE Ec and CcmE Bj were able to bind heme (Fig. 1 A, lanes 2 and 3, respectively). (asm.org)
  • Purified holoSeShp and holoSeHtsA bind Fe(II)-protoporphyrin IX (heme) and Fe(III)-protoporphyrin IX (hemin) in a 1:1 stoichiometry, respectively, and are designated hemoSeShp and hemiSeHtsA. (biomedcentral.com)
  • Turnover of catalase heme and apoprotein moieties in cotyledons of sunflower seedlings. (biomedsearch.com)
  • The turnover of catalase apoprotein and catalase heme was studied in cotyledons of sunflower (Helianthus annuus L.) seedlings by density labeling of apoprotein and radioactive labeling of heme moieties. (biomedsearch.com)
  • Following isopycnic centrifugation of catalase purified from cotyledons of 5-day-old seedlings, superimposition curve fitting was used to determine the amounts of radioactive heme moieties in native and density-labeled catalase. (biomedsearch.com)
  • Data from these determinations indicated that turnover of catalase heme and apoprotein essentially was coordinate. (biomedsearch.com)
  • The AlphaLISA ® immunoassay kit for human heme oxygenase 2 (HO-2) enables the quantitative determination of human HO-2 in serum, buffered solution, and cell culture supernatants using a homogeneous AlphaLISA assay (no wash steps). (perkinelmer.com)