Table 4.
Comparison of biophysical and functional properties of two phosphomimetic cytochrome c mutants with respect to the native phosphorylated protein.
|
in vivo pY48 Cc [110], [96] |
Y48E Cc [154], [126] |
Y48pCMF Cc [144], [116] |
|
|---|---|---|---|
| Detection by anti-pTyr | Yes | No [154], [126] |
No [144], [116] |
| E’0, pH 7.0 (mV) | – | 192.0 ± 5.0 [154], [126] 187.3 ± 0.8 [162], [130] |
208.5 ± 0.3 [144], [116] |
| Alkaline transition (pKa) | 7.0 [162], [130] |
6.3 [144], [116] |
|
| Oxygen consumption, Vmax (% of diminished capacity) | 50% | 30% [154], [126] |
60% [114], [100] |
| CcO activity, Km values (μM) | 3.0 | 3.7 [154], [126] |
– |
| Caspase activity | – | Unable to activate caspase-3 [154], [126] Decrease by 60% (ca.) compared to WT [162], [130] |
Decrease by 47.7% compared to WT [114], [100] |
| Bound to cardiolipin | – | 30% lower affinity [154], [126] |
27% more affinity [114], [100] |
| Peroxidase activity | – | Cc peroxidase activity only inducible at high cardiolipin concentration [154], [126] Larger than WT in the absence of CL [162], [130] |
In the absence of CL, the mutant shows 3 times more activity than WT [114], [100] In the presence of CL, the peroxidase activity increases twice as much as in the absence of CL [114], [100] |
– : Not available.