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. Author manuscript; available in PMC: 2012 Apr 8.
Published in final edited form as: J Mol Biol. 2011 Feb 3;407(4):477–491. doi: 10.1016/j.jmb.2011.01.055

Table 3.

Apparent dissociation constants (Kd) for the dialyzable zinc in σE/ChrR complexes containing wild type or variant ChrR proteins1

ChrR Protein
Kd (M)
Relative Affinity
WT 4.6 × 10−10 1.00
H141A 9.7 × 10−10 0.48
H143A 5.6 × 10−9 0.08
E147A 1.6 × 10−8 0.03
H177A 5.1 × 10−9 0.09
C187A 3.9 × 10−10 1.16
C189A 3.9 × 10−10 1.16
C187S 5.1 × 10−9 0.09
C189S 1.1 × 10−9 0.04
1

Apparent Kd values were calculated based on the dissociation constant of Zinbo-5 (Kd = 1.3 × 10−9 M), as described in materials and methods. Values in “Relative Affinity” column were calculated by dividing Kd value of σE/ChrR complexes containing wild type ChrR to those measured for those containing the indicated variant ChrR protein. Experiments were conducted in three separate trials with separate protein preparations. Results shown are representative data from one experimental trial. In each trial, similar trends in relative affinity for zinc were observed between samples.