EC Number   |
Natural Substrates |
|---|
    1.13.11.49 | chloride + O2 |
- |
| 1.13.11.49 | chloride + O2 |
chlorite dismutase catalyzes O2 release from chlorite with exquisite efficiency and specificity |
| 1.13.11.49 | chloride + O2 |
chlorite dismutase is a unique heme enzyme which transforms chlorite to chloride and molecular oxygen |
| 1.13.11.49 | chlorite |
- |
| 1.13.11.49 | chlorite |
catalytic mechanism via ferryl species and ClO--anion |
| 1.13.11.49 | chlorite |
the heme enzyme rapidly converts chlorite to chloride and O2, suggesting a simple approach to overcoming both the technical difficulties in the systematic variation of the O2 concentration and its modest solubility |
| 1.13.11.49 | more |
although its sequence is highly similar to functional chlorite dismutases, the HemQ protein has no steady state reactivity with chlorite, very modest reactivity with H2O2 or peracetic acid, and no observable transient intermediates |
| 1.13.11.49 | more |
upon reduction of chlorite, hypochlorite is formed and kept in the reaction sphere for recombination with the oxoiron(IV) group of Compound I. Approximately one molecule of HOCl per 100 full cycles escapes and reacts with both the prosthetic group and the protein moiety, leading to irreversible inactivation of Cld is observed which is more pronounced with an increase in pH. HOCl traps like methionine can rescue the enzyme from inactivation |
