Table 2.
Kinetic and ET parameters for the reactions of native and mutant amicyanins with O-quinol MADH
| Reaction Parameters | Native amicyanina | M98A amicyanin | M98Q amicyanin |
|---|---|---|---|
| k3 30°C (s−1) | 9.8 | 9.6 | 0.22 |
| Kd (uM) | 5 | 4 | 5 |
| ΔGo (kJ/mol) | −3.37±0.08 | −3.37±0.08 | −3.47±0.09 |
| λ (kJ/mol)b | 222±10 | 202±7 | 261±6 |
| λ (eV) | 2.30±0.10 | 2.09± 0.08 | 2.70±0.07 |
| HAB (cm−1) | 12±7 | 6.1±2 | 12±4 |
| r (Å) for β=1.0 Å−1 | 9.5 | 10.8±0.7 | 9.6±0.6 |
a
Taken from (14). In that reference a range of values of ΔGo was used to yield a range of values of λ because at that time it was uncertain as to whether it was most appropriate to use the Em value of free amicyanin or amicyanin in complex with MADH. The data in this table were recalculated using what is now known to be the appropriate ΔGo, as well as a λ value of 1.0 Å−1 which is generally accepted as reasonable for protein β sheets (41).
b
λ is sometimes expressed in units of kJ/mol and sometimes as eV so both values are given.