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. Author manuscript; available in PMC: 2015 Jul 17.
Published in final edited form as: J Biol Inorg Chem. 2010 Aug 14;15(8):1341–1352. doi: 10.1007/s00775-010-0694-2

Table 4.

Rate constants for iron release from FeChTF and His349 FeChTF mutants bound to the glycosylated, N-terminal hexa-His-tagged soluble recombinant transferrin receptor (residues 121–760) (sTFR)

Construct (FeChTF + sTFR) Conformational event k1 (min−1)a Fold difference control Iron release k2 (min−1)a Fold difference control
Controlb (N = 32) 20.6 ± 1.2 7.2 ± 0.4
H349A (N = 5) 9.2 ± 0.8 2.2 × slower 1.4 ± 0.5 5 × slower
H349Dc (N = 3) 11.3 ± 1.6 1.8 × slower
H349K (N = 5) 1.9 ± 0.2 10.8 × slower 1.9 ± 0.2 4 × slower
H349L (N = 3) 14.4 ± 0.8 1.4 × slower 1.8 ± 0.8 4 × slower
H349W (N = 3) 5.9 ± 1.6 1.2 × slower
H349Y (N = 3) 5.6 ± 0.6 1.3 × slower
a

Averages and 95% confidence intervals for kinetic runs performed on N = 3–32 different days. Each day three kinetic traces were averaged before fitting

b

From [6]

c

Note that not all the iron was removed from the H349D mutant, as indicated by urea gel analysis (Fig. 1b)