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. Author manuscript; available in PMC: 2010 Jul 16.
Published in final edited form as: Biochemistry. 2002 Mar 26;41(12):3991–4001. doi: 10.1021/bi011922x

Figure 3.

Figure 3

The mI = −1/2 line from the S-band EPR (3.5 GHz) of Cu2+ bound to 15N-labeled HGGGW and PHGGGWGQ. For HGGGW, a change in multiplet structure is observed only when the first two glycines are 15N-labeled, demonstrating that these nitrogens coordinate Cu2+. The vertical lines drawn from the most prominent features of the unlabeled spectra are included to guide the eye. The bottom two spectra are simulations where sim. 1 is for three equivalent 14N (aN = 13 G) and a hydrogen (aH = 10 G) and sim. 2 has one 14N replaced with an 15N. PHGGGWGQ shows the same pattern as HGGGW, indicating that the first two glycines coordinate to the copper center.