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Information on EC 1.11.1.B2 - chloride peroxidase (vanadium-containing) and Organism(s) Curvularia inaequalis and UniProt Accession P49053
for references in articles please use BRENDA:EC1.11.1.B2preliminary BRENDA-supplied EC number
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1.11.1.B2 chloride peroxidase (vanadium-containing)Specify your search results
Word Map
- 1.11.1.B2
- inaequalis
-
curvularia
- vanadate
- halide
-
bromoperoxidase
-
chlorination
-
vhpos
-
meroterpenoids
- glucose-6-phosphatase
- nodosum
-
ascophyllum
-
corallina
- prenyltransferase
-
peroxo
-
vanadiumv
-
bipyramidal
- seaweeds
-
td-dft
- diagnostics
- synthesis
The taxonomic range for the selected organisms is: Curvularia inaequalis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
vanadium chloroperoxidase, vanadium-dependent haloperoxidase, vanadium haloperoxidase, vanadium-dependent chloroperoxidase, vanadium-containing chloroperoxidase, naph1, mcl24, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
vanadium chloroperoxidase
-
vCPO
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
RH + Cl- + H2O2 + H+ = RCl + 2 H2O
QM/MM calculations are used to study the structural properties, ground state energies, NMR and UVvis spectra of different models of the resting states of the vanadium dependent chloroperoxidase
RH + Cl- + H2O2 + H+ = RCl + 2 H2O
biosynthesis of hypochlorite proceeds in two steps: H2O2 activation on the vanadium center to form an end-on V(V)-hydroperoxo complex, followed by OH+ transfer from hydroperoxo to chloride on the vanadium center to form hypochlorite. The initial reaction starts with a proton transfer from H2O2 to the equatorial OH group of the VV(O)2(OH)2- active site, followed by hydroperoxo binding and water release to form the highly stable vanadium-hydroperoxo-dioxo-hydroxo complex. A further proton transfer from an active-site His or Lys residue can lead to the vanadium-peroxo-hydroxo-oxo complex, which is assign as a dead-end complex unable to react further to hypochlorite products. The mechanisms are considered under various protonation state, and the most effective is the one with His404 singly protonated. Vanadium is a spectator ion that does not change its oxidation state during the reaction mechanism but holds and positions the H2O2 substrate and guides its proton-relay steps through its oxo and hydroxo ligands. The reaction is highly sensitive to local changes in the protonation state. The oxygen atom of HOCl exclusively derives from H2O2
RH + Cl- + H2O2 + H+ = RCl + 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
SYSTEMATIC NAME
IUBMB Comments
chloride:hydrogen-peroxide oxidoreductase (vanadium-containing)
-
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
1,1-dimethyl-4-chloro-3,5-cyclohexanedione + Cl- + H2O
?
-
-
-
?
Cl- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
i.e. monochlorodimedone
-
-
?
monochlorodimedone + Br- + H2O2
monobromo-monochlorodimedone + H2O
-
-
-
?
monochlorodimedone + chloride + H2O2 + H+
dichlorodimedone + H2O
-
-
-
?
styrene + KBr + H2O2
2-bromo-1-phenylethan-1-ol + 2-phenyloxirane + 2 H2O
-
-
-
?
styrene + KCl + H2O2
2-chloro-1-phenylethan-1-ol + 2 H2O
-
-
-
?
[(1E)-prop-1-en-1-yl]benzene + KBr + H2O2
(1R,2R)-2-bromo-1-phenylpropan-1-ol + 2 H2O
-
-
-
?
[(1Z)-prop-1-en-1-yl]benzene + KBr + H2O2
(1R,2S)-2-bromo-1-phenylpropan-1-ol + 2 H2O
-
-
-
?
1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane + Cl- + H2O2
additional information
-
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
i.e. monochlorodimedone
-
-
?
Br- + H2O2 + 1,1-dimethyl-4-chloro-3,5-cyclohexanedione
?
i.e. monochlorodimedone, brominating activity of chloroperoxidase
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
-
-
?
monochlorodimedon + Cl- + H2O2
dichlorodimedon + H2O
-
-
-
?
1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane + Cl- + H2O2
additional information
-
-
uncleaved chlorinated derivatives of 1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane + 1-chloro-4-ethoxy-3-methoxybenzene + 1,2-dichloro-4-ethoxy-5-methoxybenzene. 1-chloro-4-ethoxy-3-methoxybenzene and 1,2-dichloro-4-ethoxy-5-methoxybenzene are cleavage products of the chlorinated derivatives of 1-(4-ethoxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)-1,3-dihydroxypropane
-
?
additional information
?
-
oxidation of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
additional information
?
-
-
oxidation of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
-
-
?
additional information
?
-
repression by addition of glucose
-
-
?
additional information
?
-
the enzyme may have a role in the natural production of high-molecular-weight chloroaromatics and in lignin breakdown
-
-
?
additional information
?
-
the alkalophilic P395D/L241V/T343A mutant of vanadium chloroperoxidase shows bactericidal and virucidal activity
-
-
?
additional information
?
-
catalytic cycle and function of the vanadium atom in the reaction mechanism, computational study using large cluster model complexes, possible pathways, and active-site protonation states, overview
-
-
-
additional information
?
-
vanadium-dependent chloroperoxidases catalyze reactions involving peroxides and chloride, bromide, or iodide 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
additional information
?
-
repression by addition of glucose
-
-
?
additional information
?
-
the enzyme may have a role in the natural production of high-molecular-weight chloroaromatics and in lignin breakdown
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
vanadate cofactor
complex hydrogen bonding around the vanadate cofactor, Atoms-in-molecules (AIM) analysis
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
vanadate
Vanadium
vanadate
the vanadate cofactor changes its protonation from quadruply protonated at pH 6.3 to triply protonated at pH 7.3 to doubly protonated at pH 8.3. In the mutant P395D/L241V/T343A, the vanadate protonation is the same at pH 5.0 and 8.3, and the cofactor is doubly protonated
Vanadium
the vanadate binding pocket seems to form a very rigid frame stabilizing oxyanion binding
Vanadium
substitution of vanadate in the active site by phosphate leads to inactivation of the enzyme. Pervanadate is bound much more strongly to the enzyme than vanadate
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. Once the V-atom reacts with H2O2 and the peroxidovanadium(V) complex forms, a different coordination environment is formed which is critical for facilitation of the catalysis under mild conditions
Vanadium
required, electronic structure of the vanadate protonation states, overview
Vanadium
the active-site vanadium(V) ion is linked to the protein via a histidine residue. Vanadium is a spectator ion that does not change its oxidation state during the reaction mechanism but holds and positions the H2O2 substrate and guides its proton-relay steps through its oxo and hydroxo ligands
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Br-
inhibition of mutant enzyme S402A between pH 3.5 and 4.5: concentrations greater than 0.2 mM inhibit, between pH 5.0 and 5.5: concentrations above 0.5 mM inhibit, between pH 6.0 and 6.3: 0.5 mM does not inhibit the mutant enzyme
Cl-
pH 4.1: mixed type inhibition with respect to H2O2, pH 3.1: competitive inhibition
NO3-
pH 5.5: competitive inhibition of the chlorination reaction with respect to chloride, uncompetitive with respect to H2O2
hydroxylamine
inhibits rVCPO both competitively and uncompetitively. The competitive inhibition constant: 0.04 mM, uncompetitive inhibition 0.08 mM
phosphate
substitution of vanadate in the active site by phosphate leads to inactivation of the enzyme. Presence of H2O2 prevents inactivation by phosphate
phosphate
substitution of vanadate in the active site by phosphate leads to inactivation. Presence of H2O2 prevents the inactivation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Km-value for Cl- is pH-dependent whereas the Km-value for Br- is hardly pH-dependent
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
oxidation of 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid)
5.5
the wild type enzyme shows maximal activity at a pH of 5.5, but at pH of 7.7, its activity is decreased a 1000fold
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 5.5
pH 3.5: about 70% of maximal activity, pH 5.5: about 45% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
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
additional information
physiological function
vanadium haloperoxidases are one of the few enzymes in nature that utilize a vanadium center and catalyze the halogenation of substrates through the biosynthesis of hypohalite. Vanadium chloroperoxidases (VCPOs) bind and activate hydrogen peroxide and in a reaction with chloride convert it into hypochlorite as a precursor for a substrate chlorination reaction
physiological function
vanadium-dependent chloroperoxidases catalyze reactions involving peroxides and chloride, bromide, or iodide ions
additional information
calculation of higher protonation states and of a distict resting state for vanadium chloroperoxidase using quantum mechanics/molecular mechanics (QM/MM), with an atom-in-molecules analysis, overview. Di- and triprotonated states are identified as being candidates for the resting state based on a comparison of relative energies. The quadprotonated states as well as some of the triprotonated states are ruled out as the resting state. Structure of the active site of vanadium chloroperoxidase (VCPO) with bound vanadate cofactor in an unprotonated state
additional information
structure of bound peroxidovanadium(V) in the active site of the vanadium-containing haloperoxidases, overview. The V-atom in the peroxidovanadium(V)-protein complex is in a distorted square pyramidal geometry (SPY-5) but the formation of this intermediate is clearly an important reason supporting the catalysis
additional information
the active-site vanadium(V)-trioxo-hydroxo species is bound to His496. It is in trigonal bipyramidal symmetry and held in position with a string of polar (hydrogen-bonding) residues including those of Lys353, Arg360, Ser402, His404, and Arg490. As such, the active site is arranged in a tight hydrogen-bonding network, and a proton relay machinery appears to be available that can bring external protons into the active site to participate in the catalytic cycle. Active-site structure, overview. Computational modeling is performed using a combination of molecular mechanics (MM), molecular dynamics (MD), and density functional theory (DFT) calculations on cluster models. One narrow channel entering the active-site pocket with a cavity on the surface, where an organic substrate can attach. The channel connects the vanadium active site with the protein surface through the space in between the His404 and Arg490 residues. Consequently, hydrogen peroxide is inserted into the cavity at the end of the channel. Analysis of the catalytic cycle
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme crystal structure analysis, PDB ID 1IDQ. Computational modeling is performed using a combination of molecular mechanics (MM), molecular dynamics (MD), and density functional theory (DFT) calculations on cluster models
vapor diffusion method. High-resolution crystal structure (1.5 A resolution) of the reaction of the phosphate monoester p-nitrophenylphosphate with apo-VCPO exhibits a trapped intermediate of the phosphohydrolase reaction
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D292A
F397H
12% of the activity of the wild-type enzyme (chlorination of monochlorodimedone), mutant enzyme shows enhancement of bromination activity under certain conditions, inactivation of the mutant enzyme by halide especially at low pH is observed during turnover
H404A
H496A
enzyme loses the ability to bind vanadate covalently, resulting in an inactive enzyme
K353A
enzyme loses the ability to effectively oxidize chloride but can still function as bromoperoxidase, no clear pH-optimum
P395D/L241V/T343A
P395T/L241V/T343A
20fold increase in brominating activity at pH 8
R360A
enzyme loses the ability to effectively oxidize chloride but can still function as bromoperoxidase
R490A
enzyme loses the ability to effectively oxidize chloride but can still function as bromoperoxidase
S402A
1.8% of the activity of wild-type enzyme (chlorination of monochlorodimedone), mutation decreases activity, mutant enzyme still catalyzes efficiently oxidation of both Cl- and Br-
D292A
chlorinating activity is drastically reduced to approximately 1%
D292A
strongly impaired in the ability to oxidize chloride but still oxidizes bromide, although inactivation occurs during turnover
H404A
strongly impaired in the ability to oxidize chloride but still oxidizes bromide, although inactivation occurs during turnover, reduced affinity for vanadium
H404A
chlorinating activity is drastically reduced to approximately 1%
P395D/L241V/T343A
100fold increase in brominating activity at pH 8
P395D/L241V/T343A
100fold increase in brominating activity at pH 8, the brominating activity at pH 5 was increased by a factor of 6
P395D/L241V/T343A
40fold increase in brominating activity at pH 8
P395D/L241V/T343A
the mutant enzyme significantly reduces the levels of all tested microbes. This mutant has a much better potential for surface cleansing formulation at pH 8 than the wild-type enzyme
P395D/L241V/T343A
mutant exhibits 5- to 100fold improved catalytic activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80
initial decrease of activity, after which the enzyme remains stable for 6.5 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
VCPO is active in chlorination and singlet oxygenation in non-ionic microemulsions
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme remains active 10 h corresponding to 125.000 turnover with respect to O2
712779
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant CPO and mutant enzymes S402A and F397H are overexpressed as apoenzyme in Saccharomyces cerevisiae
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces cerevisiae
recombinant CPO and mutant enzymes S402A and F397H are overexpressed as apoenzyme in Saccharomyces cerevisiae
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
the observed bactericidal and virucidal activity of the alkalophilic P395D/L241V/T343A mutant of vanadium chloroperoxidase is an important step forward in the application of this robust enzyme as a component in disinfection formulations
synthesis
enzyme converts both aromatic and aliphatic alkenes into the corresponding halohydrins. Variation of pH value and addtion of ethanol as solvent leads to variation of product mixtures
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
ten Brink, H.B.; Dekker, H.L.; Schoemaker, H.E.; Wever, R.
Oxidation reactions catalyzed by vanadium chloroperoxidase from Curvularia inaequalis
J. Inorg. Biochem.
80
91-98
2000
Curvularia inaequalis (P49053), Curvularia inaequalis
Barnett, P.; Kruitbosch, D.L.; Hemrika, W.; Dekker, H.L.; Wever, R.
The regulation of the vanadium chloroperoxidase from Curvularia inaequalis
Biochim. Biophys. Acta
1352
73-84
1997
Curvularia inaequalis (P49053), Curvularia inaequalis
Renirie, R.; Hemrika, W.; Wever, R.
Peroxidase and phosphatase activity of active-site mutants of vanadium chloroperoxidase from the fungus Curvularia inaequalis. Implications for the catalytic mechanisms
J. Biol. Chem.
275
11650-11657
2000
Curvularia inaequalis (P49053), Curvularia inaequalis
Hemrika, W.; Renirie, R.; Macedo-Ribeiro, S.; Messerschmidt, A.; Wever, R.
Heterologous expression of the vanadium-containing chloroperoxidase from Curvularia inaequalis in Saccharomyces cerevisiae and site-directed mutagenesis of the active site residues His496, Lys353, Arg360, and Arg490
J. Biol. Chem.
274
23820-23827
1999
Curvularia inaequalis (P49053), Curvularia inaequalis
Simons, B.H.; Barnett, P.; Vollenbroek, E.G.M.; Dekker, H.L.; Muijsers, A.O.; Messerschmidt, A.; Wever, R.
Primary structure and characterization of the vanadium chloroperoxidase from the fungus Curvularia inaequalis
Eur. J. Biochem.
229
566-574
1995
Curvularia inaequalis (P49053), Curvularia inaequalis
Van Schijndel, J.W.; Barnett, P.; Roelse, J.; Vollenbroek, E.G.; Wever, R.
The stability and steady-state kinetics of vanadium chloroperoxidase from the fungus Curvularia inaequalis
Eur. J. Biochem.
225
151-157
1994
Curvularia inaequalis (P49053), Curvularia inaequalis
Macedo-Ribeiro, S.; Hemrika, W.; Renirie, R.; Wever, R.; Messerschmidt, A.
X-ray crystal structures of active site mutants of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis
J. Biol. Inorg. Chem.
4
209-219
1999
Curvularia inaequalis (P49053), Curvularia inaequalis
Ortiz-Bermudez, P.; Srebotnik, E.; Hammel, K.E.
Chlorination and cleavage of lignin structures by fungal chloroperoxidases
Appl. Environ. Microbiol.
69
5015-5018
2003
Leptoxyphium fumago, Curvularia inaequalis (P49053)
Tanaka, N.; Hasan, Z.; Wever, R.
Kinetic characterization of active site mutants Ser402Ala and Phe397His of vanadium chloroperoxidase from the fungus Curvularia inaequalis
Inorg. Chim. Acta
356
288-296
2003
Curvularia inaequalis (P49053)
-
Tanaka, N.; Wever, R.
Inhibition of vanadium chloroperoxidase from the fungus Curvularia inaequalis by hydroxylamine, hydrazine and azide and inactivation by phosphate
J. Inorg. Biochem.
98
625-631
2004
Curvularia inaequalis (P49053), Curvularia inaequalis
Hasan, Z.; Renirie, R.; Kerkman, R.; Ruijssenaars, H.J.; Hartog, A.F.; Wever, R.
Laboratory-evolved vanadium chloroperoxidase exhibits 100-fold higher halogenating activity at alkaline pH: catalytic effects from first and second coordination sphere mutations
J. Biol. Chem.
281
9738-9744
2006
Curvularia inaequalis (P49053), Curvularia inaequalis
de Macedo-Ribeiro, S.; Renirie, R.; Wever, R.; Messerschmidt, A.
Crystal structure of a trapped phosphate intermediate in vanadium apochloroperoxidase catalyzing a dephosphorylation reaction
Biochemistry
47
929-934
2008
Curvularia inaequalis (P49053), Curvularia inaequalis
Renirie, R.; Dewilde, A.; Pierlot, C.; Wever, R.; Hober, D.; Aubry, J.M.
Bactericidal and virucidal activity of the alkalophilic P395D/L241V/T343A mutant of vanadium chloroperoxidase
J. Appl. Microbiol.
105
264-270
2008
Curvularia inaequalis (P49053)
Zhang, Y.; Gascon, J.A.
QM/MM investigation of structure and spectroscopic properties of a vanadium-containing peroxidase
J. Inorg. Biochem.
102
1684-1690
2008
Curvularia inaequalis (P49053)
Hoogenkamp, M.A.; Crielaard, W.; ten Cate, J.M.; Wever, R.; Hartog, A.F.; Renirie, R.
Antimicrobial activity of vanadium chloroperoxidase on planktonic Streptococcus mutans cells and Streptococcus mutans biofilms
Caries Res.
43
334-338
2009
Curvularia inaequalis (P49053)
Winter, J.; Moore, B.
Exploring the chemistry and biology of vanadium-dependent haloperoxidases
J. Biol. Chem.
284
18577-18581
2009
Alternaria didymospora (P79087), Curvularia inaequalis (P49053)
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
Curvularia inaequalis (P49053)
Renirie, R.; Charnock, J.M.; Garner, C.D.; Wever, R.
Vanadium K-edge XAS studies on the native and peroxo-forms of vanadium chloroperoxidase from Curvularia inaequalis
J. Inorg. Biochem.
104
657-664
2010
Curvularia inaequalis (P49053), Curvularia inaequalis
Renirie, R.; Pierlot, C.; Wever, R.; Aubry, J.
Singlet oxygenation in microemulsion catalysed by vanadium chloroperoxidase
J. Mol. Catal. B
56
259-264
2009
Curvularia inaequalis (P49053)
-
Persoon, I.F.; Hoogenkamp, M.A.; Bury, A.; Wesselink, P.R.; Hartog, A.F.; Wever, R.; Crielaard, W.
Antimicrobial effect of a modified vanadium chloroperoxidase on Enterococcus faecalis biofilms at root canal pH
J. Endod.
39
1035-1038
2013
Curvularia inaequalis (P49053)
Dong, J.J.; Fernandez-Fueyo, E.; Li, J.; Guo, Z.; Renirie, R.; Wever, R.; Hollmann, F.
Halofunctionalization of alkenes by vanadium chloroperoxidase from Curvularia inaequalis
Chem. Commun. (Camb.)
53
6207-6210
2017
Curvularia inaequalis (P49053), Curvularia inaequalis
Gupta, R.; Hou, G.; Renirie, R.; Wever, R.; Polenova, T.
51V NMR crystallography of vanadium chloroperoxidase and its directed evolution P395D/L241V/T343A mutant protonation environments of the active site
J. Am. Chem. Soc.
137
5618-5628
2015
Curvularia inaequalis (P49053)
Mubarak, M.; Gerard, E.; Blanford, C.; Hay, S.; De Visser, S.
How do vanadium chloroperoxidases generate hypochlorite from hydrogen peroxide and chloride? A computational study
ACS Catal.
10
14067-14079
2020
Curvularia inaequalis (P49053)
-
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
Curvularia inaequalis (P49053)
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