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. Author manuscript; available in PMC: 2014 Oct 15.
Published in final edited form as: Biochemistry. 2013 Oct 1;52(41):10.1021/bi400597v. doi: 10.1021/bi400597v

Figure 3.

Figure 3

Left: kinetic mechanism of CueR interactions with a specific DNA, which includes the protein (P), DNA (D), two protein–DNA complexes that differ in protein binding modes (I and I′ ), and the rate constants for the kinetic processes. [P]: protein concentration. Between k2a and k2b, the direct substitution process k2a is dominant for holo-CueR–DNA interactions, whereas the assisted dissociation process k2b is dominant for apo-CueR–DNA interactions. Right: the kinetic parameters. The rate constants for CueR (holo) binding and unbinding with nonspecific DNA are k1 = 0.016 ± 0.001 nM−1 s−1 and k−1 = 5.9 ± 0.1 s−1; other kinetic processes do not occur to nonspecific DNA (35).