Table 5.
EPR parameters obtained from simulation of EPR spectra of Cu(II)-protein solutions.
gx | gy | gz | A∥ (10−4 cm−1) | f=gz/ A∥ (cm) | ||
---|---|---|---|---|---|---|
[a] GRα3D H3 | 75% A | 2.05 | 2.04 | 2.27 | 166 | 136.8 |
25% B | 2.05 | 2.03 | 2.22 | 149 | 149.0 | |
[a] GRα3D H4 | 50% A | 2.012 | 2.04 | 2.26 | 158 | 143.0 |
50% B | 2.04 | 2.03 | 2.23 | 188 | 119.6 | |
[a] GRα3D H2DH | N/A | 2.06 | 2.03 | 2.27 | 162 | 140.2 |
[a] GRα3D H3D | N/A | 2.04 | 2.04 | 2.26 | 168 | 134.5 |
[b] Cu-only SOD | N/A | 2.05 | 2.05 | 2.26 | ∼140 | 161.4 |
[c] Cu-(Fe) SOD | N/A | 2.05 | 2.05 | 2.37 | 136 | 174.3 |
X-band EPR spectra recorded at 100 K on solutions of 1 mM CuCl2 and 2 mM protein in 50 mM HEPES buffer containing 30% glycerol at pH 7.5, 9.3 GHz, 20.5 mW, 1 G.
Spagnolo et al., J. Biol. Chem., 2004, 33447–33455. X-band EPR spectra of a Cu-only SOD from Mycobacterium tuberculosis
Kardinahl et al., Biol. Chem., 2000, 381, 1089–1101. X-band EPR spectra recorded at 10 K of a copper-substituted FeSOD from the archaeon Acidianus ambivalens in Tris/HCl buffer at pH 7, 9.6452 GHz, 20 mW, and 10.0 G.