Bromide peroxidase

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Bromide peroxidase
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Bromoperoxidase dodekamer from Corallina pilulifera , an example of a vanadium bromoperoxidase ( PDB: 1UP8 )
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EC no. 1.11.1.18
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Bromide peroxidase (EC 1.11.1.18, bromoperoxidase, haloperoxidase (ambiguous), eosinophil peroxidase ) is a family of enzymes with systematic name bromide:hydrogen-peroxide oxidoreductase. These enzymes catalyse the following chemical reaction: [1] [2] [3]

Contents

HBr + H2O2 HOBr + H2O

The HOBr is a potent brominating agent. The many organobromine compounds observed in marine environments are the products of reaction with this oxidized form of bromine.

Bromo peroxidases of red and brown marine algae ( Rhodophyta and Phaeophyta ) contain vanadate (vanadium bromoperoxidase). Otherwise vanadium is unusual cofactor in biology. [4] By virtue of this family of enzymes, a variety of brominated natural products have been isolated from marine sources.

Related chloroperoxidase enzymes effect chlorination. In the nomenclature of haloperoxidase, bromoperoxidases classically are unable to oxidize chloride at all. For example, eosinophil peroxidase appears to prefer bromide over chloride, yet is not considered a bromoperoxidase because it is able to use chloride.

Muricidae (was Murex ) spp. snails have a bromoperoxidase used to produce Tyrian purple dye. The enzyme is very specific to bromide and physically stable, but has not been characterized as to its active site metal. As of 2019, no specific gene has been assigned to such an enzyme in the snail genome. [5] Such an activity is probably provided by symbiotic Bacillus bacteria instead. [6] The identified enzyme belongs to the alpha/beta hydrolase superfamily; a structure for a similar bromoperoxidase is available as PDB: 3FOB . It runs on a catalytic triad of Ser 99, Asp 229 and His 258 and does not require metal cofactors. [7]

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<span class="mw-page-title-main">Bromine</span> Chemical element, symbol Br and atomic number 35

Bromine is a chemical element with the symbol Br and atomic number 35. It is a volatile red-brown liquid at room temperature that evaporates readily to form a similarly coloured vapour. Its properties are intermediate between those of chlorine and iodine. Isolated independently by two chemists, Carl Jacob Löwig and Antoine Jérôme Balard, its name was derived from the Ancient Greek βρῶμος (bromos) meaning "stench", referring to its sharp and pungent smell.

<span class="mw-page-title-main">Haloalkane</span> Group of chemical compounds derived from alkanes containing one or more halogens

The haloalkanes are alkanes containing one or more halogen substituents. They are a subset of the general class of halocarbons, although the distinction is not often made. Haloalkanes are widely used commercially. They are used as flame retardants, fire extinguishants, refrigerants, propellants, solvents, and pharmaceuticals. Subsequent to the widespread use in commerce, many halocarbons have also been shown to be serious pollutants and toxins. For example, the chlorofluorocarbons have been shown to lead to ozone depletion. Methyl bromide is a controversial fumigant. Only haloalkanes that contain chlorine, bromine, and iodine are a threat to the ozone layer, but fluorinated volatile haloalkanes in theory may have activity as greenhouse gases. Methyl iodide, a naturally occurring substance, however, does not have ozone-depleting properties and the United States Environmental Protection Agency has designated the compound a non-ozone layer depleter. For more information, see Halomethane. Haloalkane or alkyl halides are the compounds which have the general formula "RX" where R is an alkyl or substituted alkyl group and X is a halogen.

<span class="mw-page-title-main">Peroxidase</span> Peroxide-decomposing enzyme

Peroxidases or peroxide reductases are a large group of enzymes which play a role in various biological processes. They are named after the fact that they commonly break up peroxides.

<span class="mw-page-title-main">Heme</span> Chemical coordination complex of an iron ion chelated to a porphyrin

Heme, or haem, is a precursor to hemoglobin, which is necessary to bind oxygen in the bloodstream. Heme is biosynthesized in both the bone marrow and the liver.

In organic chemistry, an aryl halide is an aromatic compound in which one or more hydrogen atoms, directly bonded to an aromatic ring are replaced by a halide. The haloarene are different from haloalkanes because they exhibit many differences in methods of preparation and properties. The most important members are the aryl chlorides, but the class of compounds is so broad that there are many derivatives and applications.

<span class="mw-page-title-main">Nitrogenase</span> Class of enzymes

Nitrogenases are enzymes (EC 1.18.6.1EC 1.19.6.1) that are produced by certain bacteria, such as cyanobacteria (blue-green bacteria) and rhizobacteria. These enzymes are responsible for the reduction of nitrogen (N2) to ammonia (NH3). Nitrogenases are the only family of enzymes known to catalyze this reaction, which is a step in the process of nitrogen fixation. Nitrogen fixation is required for all forms of life, with nitrogen being essential for the biosynthesis of molecules (nucleotides, amino acids) that create plants, animals and other organisms. They are encoded by the Nif genes or homologs. They are related to protochlorophyllide reductase.

A bromide ion is the negatively charged form (Br) of the element bromine, a member of the halogens group on the periodic table. Most bromides are colorless. Bromides have many practical roles, being found in anticonvulsants, flame-retardant materials, and cell stains. Although uncommon, chronic toxicity from bromide can result in bromism, a syndrome with multiple neurological symptoms. Bromide toxicity can also cause a type of skin eruption, see potassium bromide. The bromide ion has an ionic radius of 196 pm.

<span class="mw-page-title-main">Hypobromous acid</span> Chemical compound

Hypobromous acid is a weak, unstable acid with chemical formula of HOBr. It is mainly produced and handled in an aqueous solution. It is generated both biologically and commercially as a disinfectant. Salts of hypobromite are rarely isolated as solids.

<span class="mw-page-title-main">Vanadium bromoperoxidase</span>

Vanadium bromoperoxidases are a kind of enzymes called haloperoxidases. Its primary function is to remove hydrogen peroxide which is produced during photosynthesis from in or around the cell. By producing hypobromous acid (HOBr) a secondary reaction with dissolved organic matter, what results is the bromination of organic compounds that are associated with the defense of the organism. These enzymes produce the bulk of natural organobromine compounds in the world.

<span class="mw-page-title-main">Hypobromite</span> Ion, and compounds containing the ion

The hypobromite ion, also called alkaline bromine water, is BrO. Bromine is in the +1 oxidation state. The Br–O bond length is 1.82 Å. Hypobromite is the bromine compound analogous to hypochlorites found in common bleaches, and in immune cells. In many ways, hypobromite functions in the same manner as hypochlorite, and is also used as a germicide and antiparasitic in both industrial applications, and in the immune system.

Bromine compounds are compounds containing the element bromine (Br). These compounds usually form the -1, +1, +3 and +5 oxidation states. Bromine is intermediate in reactivity between chlorine and iodine, and is one of the most reactive elements. Bond energies to bromine tend to be lower than those to chlorine but higher than those to iodine, and bromine is a weaker oxidising agent than chlorine but a stronger one than iodine. This can be seen from the standard electrode potentials of the X2/X couples (F, +2.866 V; Cl, +1.395 V; Br, +1.087 V; I, +0.615 V; At, approximately +0.3 V). Bromination often leads to higher oxidation states than iodination but lower or equal oxidation states to chlorination. Bromine tends to react with compounds including M–M, M–H, or M–C bonds to form M–Br bonds.

Chloride peroxidase (EC 1.11.1.10) is a family of enzymes that catalyzes the chlorination of organic compounds. This enzyme combines the inorganic substrates chloride and hydrogen peroxide to produce the equivalent of Cl+, which replaces a proton in hydrocarbon substrate:

In enzymology, an alkylhalidase (EC 3.8.1.1) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Animal heme-dependent peroxidases</span>

Animal heme-dependent peroxidases is a family of peroxidases. Peroxidases are found in bacteria, fungi, plants and animals. On the basis of sequence similarity, a number of animal heme peroxidases can be categorized as members of a superfamily: myeloperoxidase (MPO); eosinophil peroxidase (EPO); lactoperoxidase (LPO); thyroid peroxidase (TPO); prostaglandin H synthase (PGHS); and peroxidasin.

Haloperoxidases are peroxidases that are able to mediate the oxidation of halides by hydrogen peroxide. Both halides and hydrogen peroxide are widely available in the environment.

Organobromine chemistry is the study of the synthesis and properties of organobromine compounds, also called organobromides, which are organic compounds that contain carbon bonded to bromine. The most pervasive is the naturally produced bromomethane.

<span class="mw-page-title-main">Vincent L. Pecoraro</span> American chemist

Vincent L. Pecoraro, professor at the University of Michigan, is a researcher in bioinorganic chemistry and inorganic chemistry. He is a specialist in the chemistry and biochemistry of manganese, vanadium, and metallacrown chemistry. He is a fellow of the American Association for the Advancement of Science

<span class="mw-page-title-main">Eosinophil peroxidase</span> Protein-coding gene in the species Homo sapiens

Eosinophil peroxidase is an enzyme found within the eosinophil granulocytes, innate immune cells of humans and mammals. This oxidoreductase protein is encoded by the gene EPX, expressed within these myeloid cells. EPO shares many similarities with its orthologous peroxidases, myeloperoxidase (MPO), lactoperoxidase (LPO), and thyroid peroxidase (TPO). The protein is concentrated in secretory granules within eosinophils. 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.

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<span class="mw-page-title-main">Vanadium cycle</span> Exchange of vanadium between continental crust and seawater

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References

  1. Butler, Alison.; Walker, J. V. (1993). "Marine haloperoxidases". Chemical Reviews. 93 (5): 1937–1944. doi:10.1021/cr00021a014.
  2. Latham, Jonathan; Brandenburger, Eileen; Shepherd, Sarah A.; Menon, Binuraj R. K.; Micklefield, Jason (2018). "Development of Halogenase Enzymes for Use in Synthesis". Chemical Reviews. 118 (1): 232–269. doi:10.1021/acs.chemrev.7b00032. PMID   28466644.
  3. Vaillancourt, Frédéric H.; Yeh, Ellen; Vosburg, David A.; Garneau-Tsodikova, Sylvie; Walsh, Christopher T. (2006). "Nature's Inventory of Halogenation Catalysts: Oxidative Strategies Predominate". Chemical Reviews. 106 (8): 3364–3378. doi:10.1021/cr050313i. PMID   16895332.
  4. Butler, A., "Vanadium haloperoxidases", Current Opinion in Chemical Biology, 1998, 2, 279-285.
  5. Benkendorff, K (23 April 2013). "Natural product research in the Australian marine invertebrate Dicathais orbita". Marine Drugs. 11 (4): 1370–98. doi:10.3390/md11041370. PMC   3705410 . PMID   23612370.
  6. Ngangbam, AK; Mouatt, P; Smith, J; Waters, DLE; Benkendorff, K (3 May 2019). "Bromoperoxidase Producing Bacillus spp. Isolated from the Hypobranchial Glands of a Muricid Mollusc Are Capable of Tyrian Purple Precursor Biogenesis". Marine Drugs. 17 (5): 264. doi: 10.3390/md17050264 . PMC   6562550 . PMID   31058830. Genbank AKQ77155.1.
  7. "Deposit 3FOB/IDP00046". Center for Structural Genomics of Infectious Diseases. Retrieved 31 May 2019.