Fig. 5: H2O2 and O2-dependent reoxidation of CuI-3SCC monitored by EPR. | Nature Communications

Fig. 5: H2O2 and O2-dependent reoxidation of CuI-3SCC monitored by EPR.

From: Controlling outer-sphere solvent reorganization energy to turn on or off the function of artificial metalloenzymes

Fig. 5

Time-dependent X-band EPR data for the reoxidation of 3SCC with O2 (A) and H2O2 (B) at 5 min (blue), 10 min (violet), 30 min (green), and 60 min (red). CuI-3SCC in B is shown as a gray trace. C The corresponding EPR intensity plot vs. time from double integrations (H2O2 = circles; O2 = stars). A 100-fold H2O2 was used in these experiments, and samples were frozen at various intervals. For O2, CuI-peptide was mixed with an equal volume of O2-saturated buffer, stirred, and then frozen at different intervals. The simulated spectra for 60-min samples are shown as insets in A and B. Final [ArCuP] = 0.5 mM. Data were collected at 77 K. pH = 6.5.

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