Skip to main content
. Author manuscript; available in PMC: 2011 Sep 21.
Published in final edited form as: Phys Chem Chem Phys. 2010 Jul 29;12(35):10270–10278. doi: 10.1039/c003606b

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
a

Rate constants and inverse lifetimes reported in μs−1; [CO] = 1.0 mM; [H2O] = 55.5 M.

b

Kinetic parameters from Goldbeck et al,12 crystal structure water occupancy from Quillin et al.15

c

Constrained during fitting procedure to a maximum (diffusion controlled) value of 0.08 μs−1.

d

Water occupancy values from high resolution crystal structure of deoxyHb tetramer.41

e

k′ ≡ (1 − nw)φgkinCO.

f

The φg values of the chains were fixed at the value measured by Birukou et al., as were kFeCO and koutCO.24

g

The α chain value for kinH2O[H2O] was fixed at the value obtained for the β chains.