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Information on EC 1.11.1.18 - bromide peroxidase
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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
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curvularia
- monochlorodimedone
- inaequalis
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vbpos
- pyrrocinia
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caldariomyces
- fumago
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alpha/beta-hydrolase
- fucus
- synthesis
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, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BPO
BPO-A1
BPO1
bpoA1
bromoperoxidase
BrPO
metal-free bromoperoxidase
nonhaem-type bromoperoxidase BPO 1a
nonhaem-type bromoperoxidase BPO 1b
nonhaem-type bromoperoxidase BPO 3
nonheme bromoperoxidase
perhydrolase
rVBPO
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enzyme which is expressed by Escherichia coli as inclusion bodies and subsequently refolded
V-BPO
V-BrPO
vanadium bromoperoxidase
vanadium-bromoperoxidase
vanadium-dependent bromoperoxidase
vanadium-dependent bromoperoxidase 2
VBPO1
VBPO2
VBrPO(AnI)
additional information
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
RH + HBr + H2O2 = RBr + 2 H2O
Brings about the bromination of a range of organic molecules, forming stable C-Br bonds. Can also act on iodide ions. The enzymes of this group contain vanadium (V) bound to the active centre. Since the actual halogenating agents are the respective hypohalous acids, vanadium-containing halide peroxidases lack substrate specificity and regioselectivity.
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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
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
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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.
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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
2,4-dibromophenol + bromide + H2O2
2,4,6-tribromophenol + 2 H2O
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-
-
?
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
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?
2-chlorodimedone + chloride + H2O2
1,1-dimethyl-4,4-dichloro-3,5-cyclohexanedione + 2 H2O
model substrate monochlorodimedone, activity of EC 1.11.1.10
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-
?
Br- + H2O2 + (3R)-3-bromo-2,6-dimethylhept-5-en-2-ol
3,5-dibromo-2,6-dimethylheptane-2,6-diol + H2O
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70% yield, at pH 6.0
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
bromochlorodimedone + ?
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i.e. monochlorodimedone
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-
?
Br- + H2O2 + 1-methoxynaphthalene
1-methoxy-4-bromonaphthalene + H2O
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-
-
-
?
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
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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
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?
Br- + H2O2 + 2,4,6-tribromophenol
1,3,6,8-tetrabromodibenzo-p-dioxin
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formation of ppb-level yields of 1,3,6,8-tetrabromodibenzo-p-dioxin through direct condensation. Additionally, 1,3,7,9-tetrabromodibenzo-p-dioxin, 1,2,4,7-tetrabromodibenzo-p-dioxin, and/or 1,2,4,8-tetrabromodibenzo-p-dioxin and 1,3,7-tribromodibenzo-p-dioxin and 1,3,8-tribromodibenzo-p-dioxin are frequently formed but at lower yields. Reaction probably proceeds via bromine shifts or Smiles rearrangements, whereas the tribromodibenzo-p-dioxins may result from subsequent debromination processes
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?
Br- + H2O2 + 2-hydroxybenzyl alcohol
2,4,6-tribromobenzyl alcohol + H2O
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-
?
Br- + H2O2 + 2-methoxyphenol
2-bromo-6-methoxyphenol + 4-bromo-6-methoxyphenol + H2O
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56% of product, in a 21/79 mixture of o-/p-regioisomers, plus 10% 2,4-dibromo-6-methoxyphenol
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?
Br- + H2O2 + 2-methylphenol
2-bromo-6-methylphenol + 4-bromo-6-methylphenol + H2O
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68% of product, in a 16/84 mixture of o-/p-regioisomers, plus 4% 2,4-dibromophenol
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?
Br- + H2O2 + 2-t-butylphenol
2-bromo-6-t-butylphenol + 4-bromo-6-t-butylphenol + H2O
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42% of product, in a 36/64 mixture of o-/p-regioisomers, plus 2% 2,4-dibromo-6-t-butylphenol
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?
Br- + H2O2 + 4-pentynoic acid
(5E)-bromomethylidenetetrahydro-2-furanone
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catalyzes the bromolactonization of 4-pentynoic acid forming (5E)-bromomethylidenetetrahydro-2-furanone. Formation of the bromofuranone likely results from an initial bromination reaction at the terminal alkyne, followed by cyclization from intermolecular nucleophilic attack by the terminal hydroxyl group
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?
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
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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
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?
Br- + H2O2 + methyl pyrrole-2-carboxylate
methyl 4-bromo-1H-pyrrole-2-carboxylate + methyl 5-bromo-1H-pyrrole-2-carboxylate + H2O
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quantitative conversion within 24 h, 94% of product in 93/7 ratio of 4-/5-substituted regioisomers
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?
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
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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
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?
Br- + H2O2 + monochlorodimedone
monobromo-monochlorodimedone + H2O
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?
Br- + H2O2 + phenol
2-bromophenol + 4-bromophenol + H2O
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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
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?
Br- + H2O2 + styrene
DL-1 -bromo-2-hydroxy-2-phenylethane + H2O
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?
Br- + H2O2 + trans-cinnamic acid
(+/-)-erythro-2-bromo-3-hydroxy-3-phenylpropionic acid + H2O
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?
Br- + H2O2 + trans-cinnamyl alcohol
(+/-)-1,3-dihydroxy-2-bromo-3-phenylpropane + H2O
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?
estradiol + 2 bromide + 2 H2O2
2,4-dibromo beta-estradiol + 4 H2O
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?
estradiol + 2 chloride + 2 H2O2
2,4-dichloro beta-estradiol + 4 H2O
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?
estradiol + chloride + H2O2
2-chloro beta-estradiol + 2 H2O
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?
estradiol + chloride + H2O2
4-chloro beta-estradiol + 2 H2O
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?
phenol + H2O2 + Br-
4-bromophenol + 2-bromophenol + H2O
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4-bromophenol + 2-bromophenol at the ratio of 4:1
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
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i.e. monochlorodimedone
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
i.e. monochlorodimedone
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
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i.e. monochlorodimedone
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
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i.e. monochlorodimedone
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
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i.e. monochlorodimedone
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
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i.e. monochlorodimedone
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
i.e. monochlorodimedone
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
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i.e. monochlorodimedone
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
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i.e. monochlorodimedone
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
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i.e. monochlorodimedone. Requirement of a catalytic triad in the halogenation mechanism
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
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i.e. monochlorodimedone
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
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i.e. monochlorodimedone
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?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
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i.e. monochlorodimedone
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?
Br- + H2O2 + aniline
o-bromoaniline + p-bromoaniline + ?
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no activity in absence of Br-
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?
Br- + H2O2 + aniline
o-bromoaniline + p-bromoaniline + ?
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in absence of Br- the enzyme oxidizes aniline via azobenzene and azoxybenzene finally into nitrobenzene
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?
monochlorodimedone + HBr + H2O2
monobromomonochlorodimenone + 2 H2O
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?
monochlorodimedone + HBr + H2O2
monobromomonochlorodimenone + 2 H2O
the monochlorodimedone stable enol form exists as an enolic anion without the ketoic isomer at reaction pH 5.0
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?
monochlorodimedone + HBr + H2O2
monobromomonochlorodimenone + 2 H2O
the monochlorodimedone stable enol form exists as an enolic anion without the ketoic isomer at reaction pH 5.0
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?
[6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid + Br- + H2O2 + H+
? + 2 H2O
the conversion of non-fluorescent APF to fluorescein through the production of HOBr by V-BrPO of is shown by increases in fluorescence following the addition of H2O2 to the enzyme assay mixture at approximately 50 s after initiation of data collection
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?
[6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid + Br- + H2O2 + H+
? + 2 H2O
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?
[6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid + Br- + H2O2 + H+
? + 2 H2O
Fragilariopsis cylindrus CCMP3323
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?
[6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid + Br- + H2O2 + H+
? + 2 H2O
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?
[6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid + Br- + H2O2 + H+
? + 2 H2O
Porosira glacialis CCMP651
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?
additional information
?
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enzyme uses hydrogen peroxide and bromide yielding molecular bromine as reagent for electrophilic hydrocarbon bromination
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?
additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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additional information
?
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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
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additional information
?
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vanadium-dependent bromoperoxidases catalyze reactions involving peroxides and bromide or iodide ions
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additional information
?
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assay method development and evaluation: assay for BrPO (and ClPO) activity, based on the fluorescent probe, [6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid [aminophenyl fluorescein (APF)], designed to selectively detect highly reactive oxygen species (hROS), overview. APF-based assays are used in different applications: (i) to demonstrate the generation of highly reactive hypohalite by the partially purified V-BrPO of the red seaweed Corallina officinalis and to establish the temperature response and pH optima for V-BrPO of Corallina officinalis, and (ii) measure BrPO activity in planktonic communities of coastal waters and investigate the size-distribution and temporal change of enzyme rates. In the APF assay, the hypohalite that generates fluorescein will potentially also react with other organic compounds if they are present, including molecules susceptible to electrophilic attack and halogenation. Bromoperoxidase concentration dependence of the dearylation of APF to fluorescein. The APF assay cannot be used to detect iodoperoxidases (IPO) activity. The enzyme from Corallina officinalis is not active with iodide and chloride
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additional information
?
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plays an important role in eliminating epiphytic organisms, especially microalgae on the surface. The activity increased during winter and spring and peaked in late spring. Functions to eliminate H2O2 compensating for catalase
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additional information
?
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strong brominating aactivity, weak chlorinating and iodating activities, catalyzes both benzylic and aromatic hydroxylations (e.g., of toluene and naphthalene)
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additional information
?
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assay method development and evaluation: assay for BrPO (and ClPO) activity, based on the fluorescent probe, [6-(4'-amino)phenoxy-3H-xanthen-3-on-9-yl]benzoic acid [aminophenyl fluorescein (APF)], designed to selectively detect highly reactive oxygen species (hROS), overview. APF-based assays are used in different applications: (i) quantify the BrPO activity in two different species of diatom, Porosira glacialis and Fragilariopsis cylindrus, and (ii) measure BrPO activity in planktonic communities of coastal waters and investigate the size-distribution and temporal change of enzyme rates. In the APF assay, the hypohalite that generates fluorescein will potentially also react with other organic compounds if they are present, including molecules susceptible to electro