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Literature summary for 1.11.1.18 extracted from

  • 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 (2018), Dalton Trans., 47, 2799 .
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
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 Ascophyllum nodosum

Metals/Ions

Metals/Ions Comment Organism Structure
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 Ascophyllum nodosum
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 Ascophyllum nodosum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
RH + HBr + H2O2 Ascophyllum nodosum
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RBr + 2 H2O
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?

Organism

Organism UniProt Comment Textmining
Ascophyllum nodosum K7ZUA3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-chloro-5,5-dimethyl-1,3-cyclohexane-dione HBr + H2O2 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 Ascophyllum nodosum ? + 2 H2O
-
?
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 Ascophyllum nodosum ?
-
-
RH + HBr + H2O2
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Ascophyllum nodosum RBr + 2 H2O
-
?

Synonyms

Synonyms Comment Organism
BPO
-
Ascophyllum nodosum
bromoperoxidase
-
Ascophyllum nodosum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
assay at Ascophyllum nodosum

Cofactor

Cofactor Comment Organism Structure
vanadate cofactor
-
Ascophyllum nodosum

General Information

General Information Comment Organism
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) Ascophyllum nodosum