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. Author manuscript; available in PMC: 2016 Oct 6.
Published in final edited form as: Biochemistry. 2015 Oct 6;54(39):6071–6081. doi: 10.1021/acs.biochem.5b00659

Figure 3.

Figure 3

A) Rates of CuSO4→T2Cu, and B) T2Cu→Ix conversion of CuA variants obtained from the Stopped-flow data. Rates in A) are similar in all variants. In B) highest rate is observed for Glu114GlyCuAAz which supports the hypothesis that the T2Cu→Ix conversion involves a conformation change of the CuA ligand loop as Gly has the most flexible backbone conformation, and thus favors such conformation change compared to the other amino acid side chains.