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Results 1 - 4 of 4
EC Number Reaction Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.B2RH + 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 763783
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.B2RH + Cl- + H2O2 + H+ = RCl + 2 H2O Brings about the chlorination of a range of organic molecules, forming stable C-Cl bonds. Can also act on bromide and iodide ions. Instead of the heem group of EC 1.11.1.10, the enzymes of this group contain vanadium (V) bound to the active centre. Since the actual halogenating agents are the respective hypohalous acids (like in the case of EC 1.11.1.10), vanadium-containing halide peroxidases lack substrate specificity and regioselectivity. -
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.B2RH + Cl- + H2O2 + H+ = RCl + 2 H2O QM/MM calculations are used to study the structural properties, ground state energies, NMR and UVย–vis spectra of different models of the resting states of the vanadium dependent chloroperoxidase 688195
Display the word mapDisplay the reaction diagram Show all sequences 1.11.1.B2RH + 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 765199
Results 1 - 4 of 4