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. Author manuscript; available in PMC: 2018 May 18.
Published in final edited form as: ACS Chem Biol. 2018 Apr 9;13(5):1388–1397. doi: 10.1021/acschembio.8b00293

Figure 6.

Figure 6

Cu(II) transfer between PccA and SenC is bidirectional and depends on the functional Cu binding motifs. (a) Cu(II) transfer was determined as in Figure 5, except that a mutant variant of PccA lacking its Cu-binding Met residues (PccA(ΔM)) was used as the Cu donor instead of native PccA. (b) Cu(II) transfer between native PccA and a mutant variant of SenC lacking its Cys residues (SenC(ΔC)). (c) Transfer of Cu(II) from SenC to PccA was determined as described in Figure 5, but in the reverse direction, using Cu-loaded SenCHis and Cu-free PccAStrep. After incubation, the mixture was loaded onto a Strep-Tactin affinity column, and SenC was recovered in the flow-through and wash fractions (W1–W5) and PccA in the elution fractions (E1–E5). The protein and Cu contents of each fraction were determined as before. (d) As in (c) except that PccA(ΔM) was used as the Cu acceptor instead of native PccA as a control for Cu transfer.