Table 1.
Kinetic parameters for MbCO and isolated HbCO α and β chains.a
Variant | kFeCO (μs−1) | kinCO[CO]c (μs−1) | koutCO (μs−1) | kinH2O[H2O] (μs−1) | koutH2O (μs−1) | nw | X-ray Structure H2O Occupancy | φg | 1− nw | k′[CO]e (μs−1) | τobs−1 (μs−1) |
---|---|---|---|---|---|---|---|---|---|---|---|
Mbb | 0.11 | (0.08) | 2.2 | 9.0 | 1.7 | 0.84 | 0.84 | 0.051 | 0.16 | 0.00064 | 0.00066 |
α Native f | 3.4 | (0.08) | 21 | 6.0g | 3.4 | 0.64 | 1.00d | 0.14 | 0.36 | 0.0040 | 0.0057 |
β Native f | 1.6 | (0.08) | 6.0 | 6.0 | 20 | 0.23 | 0.00d | 0.22 | 0.77 | 0.014 | 0.011 |
Rate constants and inverse lifetimes reported in μs−1; [CO] = 1.0 mM; [H2O] = 55.5 M.
Constrained during fitting procedure to a maximum (diffusion controlled) value of 0.08 μs−1.
Water occupancy values from high resolution crystal structure of deoxyHb tetramer.41
k′ ≡ (1 − nw)φgkinCO.
The φg values of the chains were fixed at the value measured by Birukou et al., as were kFeCO and koutCO.24
The α chain value for kinH2O[H2O] was fixed at the value obtained for the β chains.