Table 3.
Kinetic Parameters for Binding of Heme to Selected Proteins
| protein | kon (μMY−1 s−1) | k−heme (s−1) | KD (μM) | reference |
|---|---|---|---|---|
| BtNosP | 5.6 × 10−3 − 2.8 × 10−2(k−heme/KD) | (2.98 ± 0.60) × 10−3 | (5.3 ± 1.2) × 10−1 | this work |
| (1.48 ± 0.19) × 10−2 | ||||
| Vc_0130 (CdpA) | ND a | 3.0 × 10−4 | ND a | 16 |
| PaPhuS | 1.8 × 10−1 | 3.6 × 10−2(KD*kon) | 2.0 × 10−1 | 56 |
| rGAPDH | 1.78 × 10−2 | 3.3 × 10−4 | 1.9 × 10−2 − 3.9 × 10−1(k−heme/kon) | 52 |
| 7.0 × 10−3 | 2.4 × 10−2 (direct measurement) | |||
| HRI | 11 | 1.5 × 10−3 | 1.4 × 10−4(k−heme/kon) | 53 |
| MhuD (first heme binding) | 14–33(k−heme/KD) | 2.53 × 10−1 | 7.6 × 10−3 | 20,57 |
| 1.03 × 10−1 | ||||
| myoglobin | 76 | 8.4 × 10−7 | 1.1 × 10−8(k−heme/kon) | 51 |
| sGC | ND a | 8.3 × 10−6b | ND a | 55 |
a
ND, not determined.
b
Ferric heme dissociation rate; ferrous heme does not dissociate upon apo-myoglobin challenge.