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Information on EC 1.11.1.18 - bromide peroxidase and Organism(s) Ascophyllum nodosum and UniProt Accession P81701
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1.11.1.18 bromide peroxidaseIUBMB Comments
Bromoperoxidases of red and brown marine algae (Rhodophyta and Phaeophyta) contain vanadate. They catalyse the bromination of a range of organic molecules such as sesquiterpenes, forming stable C-Br bonds. Bromoperoxidases also oxidize iodides.
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Word Map
- 1.11.1.18
-
bromination
- chloroperoxidase
- nodosum
- ascophyllum
-
corallina
- aureofaciens
- halide
- pilulifera
-
curvularia
- monochlorodimedone
- inaequalis
-
vbpos
- pyrrocinia
-
caldariomyces
- fumago
-
alpha/beta-hydrolase
- fucus
- synthesis
The taxonomic range for the selected organisms is: Ascophyllum nodosum
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
v-brpo, perhydrolase, bpo-a1, vanadium-dependent bromoperoxidase, bromoperoxidase ii, bromoperoxidase-catalase, bpo-a2, vanadium-containing bromoperoxidase, vbrpo, v-bpo, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BPO
bromoperoxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
RH + HBr + H2O2 = RBr + 2 H2O
the catalytic cycle imposes changes in the coordination geometry of the vanadium to accommodate the peroxidovanadium(V) intermediate in an environment of as a distorted square pyramidal geometry. During the catalytic cycle, this intermediate converts to a trigonal bipyramidal intermediate before losing the halogen and forming a tetrahedral vanadium-protein intermediate. The catalysis is facilitated by a proton-relay system supplied by the second sphere coordination environment, and the changes in the coordination environment of the vanadium(V) making this process unique among protein catalyzed processes. The active site is very tightly regulated with only minor changes in the coordination geometry. The coordination geometry in the protein structures deviates from that found for both small molecules crystallized in the absence of protein and the reported functional small molecule model compounds. The catalytic mechanism for oxidation of organic substrates catalyzed by haloperoxidases does not change the oxidation state of the vanadium(V) although the vanadium is present as protein bound intermediate with a coordination number altering from four to six
RH + HBr + H2O2 = RBr + 2 H2O
proposed states at the bromoperoxidase active site involved in primary product formation and secondary reaction consuming hypobromous acid in the absence of an accepting organic substrate, overview. At the bromoperoxidase II binding site, dihydrogen orthovanadate most likely encounters reactivity in between diffusion-controlled solution chemistry and aligned reactant pairs. According to steady kinetic data, hydrogen peroxide binding to VBrPO(AnII) is one of the rate-determining steps. The energy required for transforming the bromoperoxidase resting state into the peroxo state must be provided by the succeeding step, which is the transfer of a peroxide oxygen atom to bromide. The least negatively charged oxygen in peroxide side-on-4, OP, is the site preferentially approached by bromide in the electronic structure model. Reaction mechanism analysis
SYSTEMATIC NAME
IUBMB Comments
bromide:hydrogen-peroxide oxidoreductase
Bromoperoxidases of red and brown marine algae (Rhodophyta and Phaeophyta) contain vanadate. They catalyse the bromination of a range of organic molecules such as sesquiterpenes, forming stable C-Br bonds. Bromoperoxidases also oxidize iodides.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Br- + H2O2 + 2-methoxyphenol
2-bromo-6-methoxyphenol + 4-bromo-6-methoxyphenol + H2O
-
56% of product, in a 21/79 mixture of o-/p-regioisomers, plus 10% 2,4-dibromo-6-methoxyphenol
-
?
Br- + H2O2 + 2-methylphenol
2-bromo-6-methylphenol + 4-bromo-6-methylphenol + H2O
-
68% of product, in a 16/84 mixture of o-/p-regioisomers, plus 4% 2,4-dibromophenol
-
?
Br- + H2O2 + 2-t-butylphenol
2-bromo-6-t-butylphenol + 4-bromo-6-t-butylphenol + H2O
-
42% of product, in a 36/64 mixture of o-/p-regioisomers, plus 2% 2,4-dibromo-6-t-butylphenol
-
?
Br- + H2O2 + methyl pyrrole-2-carboxylate
methyl 4-bromo-1H-pyrrole-2-carboxylate + methyl 5-bromo-1H-pyrrole-2-carboxylate + H2O
-
quantitative conversion within 24 h, 94% of product in 93/7 ratio of 4-/5-substituted regioisomers
-
?
Br- + H2O2 + phenol
2-bromophenol + 4-bromophenol + H2O
-
69% of product, in a 91/9 mixture of o-/p-regioisomers, plus 3% 2,4-dibromo-6-methylphenol and some 2,4,6-tribromophenol
-
?
2-chloro-5,5-dimethyl-1,3-cyclohexane-dione HBr + H2O2
? + 2 H2O
2-chloro-5,5-dimethyl-1,3-cyclohexane-dione (mcd) is the standard substrate for the determination of haloperoxidase activity using H2O2 as the oxidant
-
-
?
Br- + H2O2 + (3R)-3-bromo-2,6-dimethylhept-5-en-2-ol
3,5-dibromo-2,6-dimethylheptane-2,6-diol + H2O
-
-
70% yield, at pH 6.0
-
?
Br- + H2O2 + 1-phenylpent-4-en-1-ol
4-bromo-1-phenylpentane-1,5-diol + 5-bromo-1-phenylpentane-1,4-diol + 2-(bromomethyl)-5-phenyltetrahydrofuran + H2O
-
-
30% yield of 4-bromo-1-phenylpentane-1,5-diol, 28% yield of 5-bromo-1-phenylpentane-1,4-diol, and 25% yield of 2-(bromomethyl)-5-phenyltetrahydrofuran, at pH 6.0
-
?
Br- + H2O2 + 5-methyl-1-phenylhex-4-en-1-ol
4-bromo-5-methyl-1-phenylhexane-1,5-diol + 2-(1-bromo-1-methylethyl)-5-phenyltetrahydrofuran + 3-bromo-2,2-dimethyl-6-phenyltetrahydro-2H-pyran + H2O
-
-
69% yield of 4-bromo-5-methyl-1-phenylhexane-1,5-diol, 6% yield of 2-(1-bromo-1-methylethyl)-5-phenyltetrahydrofuran, and 9% yield of 3-bromo-2,2-dimethyl-6-phenyltetrahydro-2H-pyran, at pH 6.0
-
?
Br- + H2O2 + methyl pyrrole-2-carboxylate
methyl 5-amino-4-bromocyclopenta-1,3-diene-1-carboxylate + methyl 5-amino-3-bromocyclopenta-1,3-diene-1-carboxylate + methyl 5-amino-3,4-dibromocyclopenta-1,3-diene-1-carboxylate + H2O
-
-
5% yield of methyl 5-amino-4-bromocyclopenta-1,3-diene-1-carboxylate, 59% yield of methyl 5-amino-3-bromocyclopenta-1,3-diene-1-carboxylate, and 5% yield of methyl 5-amino-3,4-dibromocyclopenta-1,3-diene-1-carboxylate, at pH 6.3 and 25°C
-
?
additional information
?
-
enzyme uses hydrogen peroxide and bromide yielding molecular bromine as reagent for electrophilic hydrocarbon bromination
-
-
?
additional information
?
-
vanadium containing bromoperoxidase mimicking (structural and/or functional) activities of vanadium(V) complexes has been reported by several groups in which the active site contains vanadium(V) coordinated to O/N donor ligands. Vanadium(V) complexes catalyze the oxidative bromination of organic substrates into useful halogenated organic compounds in the presence of halide and H2O2 in mild acid medium, just like natural VBrPO enzymes and hence, these are considered as models for VBrPO enzymes. Synthesis, crystal structure, DFT calculations, protein interaction, anticancer potential and bromoperoxidase mimicking activity of oxidoalkoxidovanadium(V) complexes: DFT calculations, protein interaction analysis, circular dichroism study, anticancer activity determination with MCF-7 cells, and determination of mitochondrial membrane potential (MMP) as well as intracellular reactive oxygen species (ROS) production, detailed overview
-
-
-
additional information
?
-
vanadium-dependent bromoperoxidases catalyze reactions involving peroxides and bromide or iodide ions
-
-
-
additional information
?
-
protein binding through the enzyme occurs primarily through hydrogen bridges and superimposed by Coulomb attraction according to thermochemical model on density functional level of theory. The strongest attractor is the arginine side chain mimic N-methylguanidinium, enhancing in positive cooperative manner hydrogen bridges toward weaker acceptors, such as residues from lysine and serine. Hydrogen peroxide activation occurs in the thermochemical model by side-on binding in orthovanadium peroxoic acid, oxidizing bromide with virtually no activation energy to hydrogen bonded hypobromous acid
-
-
-
additional information
?
-
-
protein binding through the enzyme occurs primarily through hydrogen bridges and superimposed by Coulomb attraction according to thermochemical model on density functional level of theory. The strongest attractor is the arginine side chain mimic N-methylguanidinium, enhancing in positive cooperative manner hydrogen bridges toward weaker acceptors, such as residues from lysine and serine. Hydrogen peroxide activation occurs in the thermochemical model by side-on binding in orthovanadium peroxoic acid, oxidizing bromide with virtually no activation energy to hydrogen bonded hypobromous acid
-
-
-
additional information
?
-
the disproportionation reaction of hydrogen peroxide is a bromidemediated reaction, i.e. V-BPO does not catalyze the formation of singlet oxygen in the absence of bromide ions
-
-
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
vanadate cofactor
required, binding structure and thermodynamics analysis, detailed overview. Every monomer binds one equivalent of orthovanadate in a cavity formed from side chains of three histidines, two arginines, one lysine, serine, and tryptophan. Hydrogen peroxide interferes with orthovanadate equilibria, providing in pH-neutral aqueous solution mono-, di-, tri-, and tetraperoxidoorthovanadates, depending on concentration and vanadate-peroxide ratio. Bromoperoxidase proteins control specificity for oxygen atom transfer to bromide to give hypobromous acid and direct the cofactor by the end of the sequence into the resting state for resuming substrate turnover in a succeeding catalytic cycle. Calculated energies for isodesmic substitution of water from hydrated orthovanadates via vanadium bonding of nitrogen compounds
-
additional information
-
the enzyme does require no additional cofactor
-
additional information
development of a comprehensive theory for cofactor bonding and bromide oxidation at the active site using an assessed electronic structure method. Three dimers interwoven in contact regions and tightened by hydrogen-bond-clamped guanidinium stacks along with regularly aligned water molecules form the basic structure of the enzyme. Intra- and intermolecular disulfide bridges further stabilize the enzyme
-
additional information
-
development of a comprehensive theory for cofactor bonding and bromide oxidation at the active site using an assessed electronic structure method. Three dimers interwoven in contact regions and tightened by hydrogen-bond-clamped guanidinium stacks along with regularly aligned water molecules form the basic structure of the enzyme. Intra- and intermolecular disulfide bridges further stabilize the enzyme
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
vanadate
in the solid state structure, every protein monomer binds one vanadate to the tele imidazole nitrogen of residue His486. In solutions of sodium orthovanadate, isoform apobromoperoxidase II recovers bromoperoxidase activity by one order of magnitude faster than apobromoperoxidase I
Vanadium
Vanadium
additional information
formation of mono- and dinuclear oxidovanadium(V) complexes of an amine-bis(phenolate) ligand with bromoperoxidase activities, synthetic routes and kinetics of the complexes, overview
Vanadium
the holoenzyme contains trigonal-bipyramidal coordinated vanadium atoms at its two active centres
Vanadium
required vanadium as a transition metal ion that readily converts among oxidations states has the potential to support catalytic processes through oxidation/reduction chemistry as well as hydrolytic chemistry. Coordination chemistry of the vanadium(V) center in the different vanadium-haloperoxidases, overview
Vanadium
-
presence of vanadium coordinated to oxygen/nitrogen either as vanadium(V) (in the native, native plus bromide, and native plus peroxide samples) or vanadium(IV) (in the reduced enzyme). There are structural changes at the metal site on reduction of the native enzyme, notably a lengthening of the average inner-shell distance and the presence of terminal oxygen together with histidine and oxygen-donating residues
Vanadium
-
the substrate bromide does not bind to active site vanadium but to a light atom, possibly carbon, in its vicinity
Vanadium
required, every monomer binds one equivalent of orthovanadate in a cavity formed from side chains of three histidines, two arginines, one lysine, serine, and tryptophan
Vanadium
the vanadium ion is ligated to the protein backbone via one histidine nitrogen donor atom, while the oxido moieties are strongly H-bonded to arginine, lysine, histidine and serine amino acids
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
vanadium-dependent haloperoxidases (VPXOs) are a class of enzymes that catalyze selective oxidation reactions for which vanadium is an essential cofactor converting halides to form halogenated organic products and water. These enzymes include chloroperoxidase and bromoperoxidase, which have very different protein sequences and sizes, but regardless the coordination environment of the active sites is constant. Coordination chemistry of the vanadium(V) center in the different vanadium-haloperoxidases, overview
physiological function
vanadium-dependent bromoperoxidases catalyze reactions involving peroxides and bromide or iodide ions
evolution
physiological function
the peroxide is the terminal oxidant for converting bromide into electrophilic bromine compounds
additional information
evolution
the enzyme belongs into a class of metalloenzymes utilizing orthovanadate as a cofactor for activating hydrogen peroxide
evolution
vanadate-dependent haloperoxidases (VHPOs) are the enzymes that catalyze the 2e- oxidation of a halide by H2O2 to the corresponding hypohalous acids, HOX. Thereby, the formed HOX can react with a broad range of organic substrates to form a diverse variety of halogenated compounds. The classification of VHPOs is based on the nature of the halides oxidized, whereby when they catalyse the oxidation of Cl-, Br- or I- in the presence of H2O2, they are designated as chloroperoxidaes (CPOs), while for the oxidation of Br- or I- they are classified as bromoperoxidases (BPOs) and for the oxidation of I- as iodoperoxidases (IPOs)
additional information
structure of bound peroxidovanadium(V) in the active site of the vanadium-containing haloperoxidases, overview
additional information
analysis of cofactor bonding and bromide oxidation at the active site, overview. Three-dimensional structure modeling of VBrPO(AnII) using the structure of isozyme VBrPO(AnI) (PDB ID 1QI9) as a template
additional information
-
analysis of cofactor bonding and bromide oxidation at the active site, overview. Three-dimensional structure modeling of VBrPO(AnII) using the structure of isozyme VBrPO(AnI) (PDB ID 1QI9) as a template
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PRXV_ASCNO
557
0
60344
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homohexamer
bromoperoxidase II comprises six identical subunits. Converging chains of N-terminal peptides are interwoven at dimer-dimer interfaces in a catenane-type manner. Guanidinium stacks between arginine side chains tighten interfaces by hydrogen bond-clamping between prolyl carboxamide and guanidinium groups, being supplemented by attractive forces from arrays of hydrogen-bonded water molecules, for overcoming like/like repulsion. 40% of the bromoperoxidase II solid state secondary structure derive from helices, 10% from beta-strands, 4% from turns, and 46% from coils. Primary and secondary enzyme structure analysis, comparison of the enzyme structure with other enzyme structures, modeled surface polarization of a VBrPO(AnII)-monomer, detailed overview. Every chain, labeled alphabetically from A to F, contains one molecule of orthovanadate. Disulfide bridges connect thiol groups from cysteine(Cys)41 and Cys77 of one chain to Cys77 and Cys41 to the proximal, linking chain A to chain F, B to C, and D to E. Intramolecular disulfide bridges are formed from Cys117 to Cys126, from Cys474 to Cys502, and from Cys603 to Cys613
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized from ammonium sulfate solutions in a form suitable for X-ray diffraction analysis. Crystals are grown by the vapour-diffusion technique using the sitting-drop method. X-ray diffraction studies show that the crystals belong to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2 with a = b = 114.3 and c = 276.0 A. The crystals diffract to at least 2.4 A resolution
structure of the enzyme is solved by single isomorphous replacement anomalous scattering X-ray crystallography at 2.0 A resolution. Crystals of the holoenzyme and the apoenzyme are obtained from 2.1 M ammonium sulfate solutions buffered at pH 8.3 and diffract to 2.4 A resolution. The crystals are stable in the X-ray beam for more than one week. They belong to the tetragonal system, space group P4(3)2(1)2, with lattice constants a ?= 114.3 A,? c = 276.0 A
purified native enzyme, hanging drop vapor diffusion method, mixing of 0.001-0.002 ml of 8 mg/ml protein solution with 0.0005-0.001 ml of reservoir solution containing 0.1 M sodium chloride, 0.01 M Tris-HCl, pH 5.5, and 25% PEG 3350 leading to monoclinic crystals, or 0.15 M potassium rhodanide, 0.01 M Tris, pH 7.5, and 19% PEG 3350 leading to hexagonal crystals, both at a temperature of 18°C, X-ray diffraction structure determination and analysis at 2.26 A resolution, molecular replacement and modeling of VBrPO(AnII) using the structure of isozyme VBrPO(AnI) (PDB ID 1QI9) as a template
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
synthesis, crystal structure, DFT calculations, protein interaction, anticancer potential and bromoperoxidase mimicking activity of oxidoalkoxidovanadium(V) complexes: DFT calculations, protein interaction analysis, circular dichroism study, anticancer activity determination with MCF-7 cells, and determination of mitochondrial membrane potential (MMP) as well as intracellular reactive oxygen species (ROS) production, detailed overview
additional information
chemical synthesis of mono- and dinuclear oxidovanadium(V) complexes of an amine-bis(phenolate) ligand with bromoperoxidase activities, synthetic routes and kinetics of the complexes, NMR studies, kinetics, and mechanism and catalytic cycle, overview. Complex [LV(O)(H2O2)] formed through the oxidation of Br- to Br+ by [LV(O)(O...Br) (H3O)]+ in the presence of H2O2/KBr, can satisfactorily catalyse the oxidative bromination of salicylaldehyde to give 5-bromosalicylaldehyde as a major product along with 3,5-dibromo-salicylaldehyde and 2,3,5-tribromosalicylaldehyde as minor products, in the presence of HClO4 in mixed solvents (H2O : MeOH : THF = 4 : 3 : 2) at 25°C. In the absence of the catalyst, the reaction mixture gives only a 4% conversion of salicylaldehyde to 5-bromosalicylaldehyde. Catalytic parameters for the bromination of salicylaldehyde by KBr/H2O2 (KBr = 40 mmol, H2O2 = 2 ml, i.e. 67 mmol) using two complexes as catalysts
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity half-life times increase along the series of buffers: phosphate
-
circular dichroism measurements showed that the secondary structure is not affected upon incubation in 4% SDS
-
denaturation did not occur upon incubation in 4 M guanidine hydrochloride
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
20°C, in 0.001 mM H2O2-incubated, MES-buffered (pH 6.22) aqueous alcoholic solution, half-life time of about 60 days
-
20°C, in 0.001 mM NaCl-incubated, MES-buffered (pH 6.22) aqueous alcoholic solution, half-life time of about 24 days
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme VBrPO(AnII) from algal powder by liquid-liquid-partitioning, dialysis, and ultracentrifugation
phenyl Sepharose column chromatography and Phenyl Sepharose gel filtration
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
immobilization of enzyme on magnetic micrometre-sized particles in quantitative yields, with up to 40% retention of initial bromoperoxidase activity. The immobilized enzyme is stable with a half-life time of about 160 days. It serves as reusable catalyst for bromide oxidation with H2O2 in up to 14 consecutive experiments. Immobilized enzyme is used for methyl pyrrole-2-carboxylate conversion into derivatives of naturally occurring compounds e.g. from Agelas oroides with product selectivity of up to 75%
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Arber, J.M.; de Boer, E.; Garner, C.D.; Hasnain, S.S.; Wever, R.
Vanadium K-edge X-ray absorption spectroscopy of bromoperoxidase from Ascophyllum nodosum
Biochemistry
28
7968-7973
1989
Ascophyllum nodosum
Tromp, M.G.; Olafsson, G.; Krenn, B.E.; Wever, R.
Some structural aspects of vanadium bromoperoxidase from Ascophyllum nodosum
Biochim. Biophys. Acta
1040
192-198
1990
Ascophyllum nodosum
Butler, A.
Vanadium haloperoxidases
Curr. Opin. Chem. Biol.
2
279-285
1998
Corallina officinalis, Ascophyllum nodosum
Rehder, D.; Schulzke, C.; Dau, H.; Meinke, C.; Hanss, J.; Epple, M.
Water and bromide in the active center of vanadate-dependent haloperoxidases
J. Inorg. Biochem.
80
115-121
2000
Ascophyllum nodosum
Waller, M.P.; Geethalakshmi, K.R.; Buehl, M.
51V NMR chemical shifts from quantum-mechanical/molecular-mechanical models of vanadium bromoperoxidase
J. Phys. Chem. B
112
5813-5823
2008
Ascophyllum nodosum (P81701)
Geethalakshmi, K.R.; Waller, M.P.; Thiel, W.; Buehl, M.
51V NMR chemical shifts calculated from QM/MM models of peroxo forms of vanadium haloperoxidases
J. Phys. Chem. B
113
4456-4465
2009
Ascophyllum nodosum (P81701)
Hartung, J.; Bruecher, O.; Hach, D.; Schulz, H.; Vilter, H.; Ruick, G.
Bromoperoxidase activity and vanadium level of the brown alga Ascophyllum nodosum
Phytochemistry
69
2826-2830
2008
Ascophyllum nodosum
Hartung, J.; Dumont, Y.; Greb, M.; Hach, D.; Koehler, F.; Schulz, H.; Casny, M.; Rehder, D.; Vilter, H.
On the reactivity of bromoperoxidase I (Ascophyllum nodosum) in buffered organic media: Formation of carbon bromine bonds
Pure Appl. Chem.
81
1251-1264
2009
Ascophyllum nodosum
-
Wischang, D.; Hartung, J.; Hahn, T.; Ulber, R.; Stumpf, T.; Fecher-Trost, C.
Vanadate(v)-dependent bromoperoxidase immobilized on magnetic beads as reusable catalyst for oxidative bromination
Green Chem.
13
102-108
2011
Ascophyllum nodosum (P81701)
-
Wischang, D.; Hartung, J.
Bromination of phenols in bromoperoxidase-catalyzed oxidations
Tetrahedron
68
9456-9463
2012
Ascophyllum nodosum (P81701)
-
Weyand, M.; Hecht, H.J.; Vilter, H.; Schomburg, D.
Crystallization and preliminary X-ray analysis of a vanadium-dependent peroxidase from Ascophyllum nodosum
Acta Crystallogr. Sect. D
52
864-865
1996
Ascophyllum nodosum (P81701), Ascophyllum nodosum
Weyand, M.; Hecht, H.; Kiess, M.; Liaud, M.; Vilter, H.; Schomburg, D.
X-ray structure determination of a vanadium-dependent haloperoxidase from Ascophyllum nodosum at 2.0 A resolution
J. Mol. Biol.
293
595-611
1999
Ascophyllum nodosum (P81701), Ascophyllum nodosum
Radlow, M.; Czjzek, M.; Jeudy, A.; Dabin, J.; Delage, L.; Leblanc, C.; Hartung, J.
X-ray diffraction and density functional theory provide insight into vanadate binding to homohexameric bromoperoxidase II and the mechanism of bromide oxidation
ACS Chem. Biol.
13
1243-1259
2018
Ascophyllum nodosum (K7ZUA3), Ascophyllum nodosum
Debnath, M.; Dolai, M.; Pal, K.; Bhunya, S.; Paul, A.; Lee, H.M.; Ali, M.
Mono- and dinuclear oxidovanadium(V) complexes of an amine-bis(phenolate) ligand with bromoperoxidase activities synthesis, characterization, catalytic, kinetic and computational studies
Dalton Trans.
47
2799
2018
Ascophyllum nodosum (K7ZUA3)
McLauchlan, C.C.; Murakami, H.A.; Wallace, C.A.; Crans, D.C.
Coordination environment changes of the vanadium in vanadium-dependent haloperoxidase enzymes
J. Inorg. Biochem.
186
267-279
2018
Ascophyllum nodosum (P81701)
Biswal, D.; Pramanik, N.; Drew, M.; Jangra, N.; Maurya, M.; Kundu, M.; Sil, P.; Chakrabarti, S.
Synthesis, crystal structure, DFT calculations, protein interaction, anticancer potential and bromoperoxidase mimicking activity of oxidoalkoxidovanadium(V) complexes
New J. Chem.
43
17783-17800
2019
Ascophyllum nodosum (P81701)
-
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