EC Number   |
Cofactor |
Reference |
|---|
    1.13.11.49 | heme |
- |
699577, 700954, 712251, 712897, 724334, 724812, 725255, 741941, 763788, 764144, 765092, 765093 |
| 1.13.11.49 | heme |
at pH 6.0, ferric Cld exhibits a Soret band maximum at 405 nm, a broad alpha/beta band envelope at 505 nm with a small shoulder at 540 nm, and a charge transfer band at 645 nm |
741914 |
| 1.13.11.49 | heme |
HemQ's equilibrium affinity for heme is in the low micromolar range. Holo-HemQ reconstituted with heme exhibits heme lysis after less than 50 turnovers with peroxide and less than 10 turnovers with chlorite. The heme-free apoprotein aggregates or unfolds over time. HemQ uses heme or porphyrin-like organic molecules as substrates. Heme in HemQ degrades in the presence of relatively small numbers of equivalents of H2O2, chlorite, or peracetic acid |
725529 |
| 1.13.11.49 | heme |
presence of one b-type heme per monomer |
743040 |
| 1.13.11.49 | heme |
resting ferric high-spin axially symmetric heme enzyme, standard reduction potential of the Fe(III)/Fe(II) couple of -126 mV at pH 7.0 |
743310 |
| 1.13.11.49 | heme |
wild-type Cld shows a variety of low- and high-spin ferric heme forms. Addition of an axial ligand, such as azide or imidazole, removes this heterogeneity almost entirely |
743149 |
| 1.13.11.49 | heme b |
- |
764186 |
| 1.13.11.49 | heme b |
contains 3.7 heme per tetramer |
685244 |
