EC Number   |
Cofactor |
Reference |
|---|
    1.11.1.11 | heme |
- |
439855, 439856, 439858, 439860, 439862, 439865, 439868, 439871, 439872, 439874, 439876, 439880, 696216, 696257, 697682, 698047, 699802, 711139, 713234, 713299, 725934, 743696, 763910, 764255, 764383, 764388, 764715, 764780, 764787, 764826, 764871, 765160, 765273, 765501, 765572, 765596, 765620, 765632, 765656, 765773 |
| 1.11.1.11 | heme |
ascorbate peroxidase binds some substrates at the gamma-heme edge |
765196 |
| 1.11.1.11 | heme |
covalent linking of Trp41 to the heme group in ascorbate peroxidase can occur on exposure of the enzyme to peroxide. A reaction mechanism involving formation of a protein radical at Trp41 is implicated to account for this observation |
685131 |
| 1.11.1.11 | heme |
determination of the redox potential for the Fe3+/Fe2+, CI/Fe3+, CI/II, and CII/Fe3+ redox couples in rsAPX and various site-directed variants by direct potentiometric titration |
685177 |
| 1.11.1.11 | heme |
one protoheme moiety per molecule |
439861 |
| 1.11.1.11 | more |
electronic, EPR, and NMR spectra are consistent with a high-spin ferric resting state for the enzyme at 298K, low temperature EPR and electronic absorption experiments indicate formation of a low-spin heme derivative at these temperatures, the midpoint reduction potential for the Fe(III)/Fe(II) redox couple, determined by spectroelectrochemistry is -159 mV vs SHE, sodium phosphate: pH 7, 25°C, 0.10 M |
439872 |
| 1.11.1.11 | more |
the enzyme may not be a heme-peroxidase |
439867 |
| 1.11.1.11 | NADPH |
- |
694642 |
