1.11.1.B6: iodide peroxidase (vanadium-containing)
This is an abbreviated version!
For detailed information about iodide peroxidase (vanadium-containing), go to the full flat file.
Reaction
Synonyms
iodooperoxidase, iodoperoxidases PcI, iodoperoxidases PcII, V-containing-haloperoxidase, vanadium-dependent haloperoxidase, vanadium-dependent iodoperoxidase, vIPO, zobellia_1262
ECTree
1.11.1.B6 iodide peroxidase (vanadium-containing)Advanced search results
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Reaction on EC 1.11.1.B6 - iodide peroxidase (vanadium-containing)
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REACTION 
REACTION DIAGRAM
COMMENTARY 
ORGANISM
UNIPROT
LITERATURE
RH + I- + H2O2 + H+ = RI + 2 H2O
Brings about the iodination of a range of organic molecules, forming stable C-I bonds. The enzymes of this group contain vanadium (V) bound to the active centre.
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RH + I- + H2O2 + H+ = RI + 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 + I- + H2O2 + H+ = RI + 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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RH + I- + H2O2 + H+ = RI + 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 + I- + H2O2 + H+ = RI + 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 + I- + H2O2 + H+ = RI + 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 + I- + H2O2 + H+ = RI + 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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