Electron paramagnetic resonance studies of the soluble CuA protein from the cytochrome ba3 of Thermus thermophilus.
The electron paramagnetic resonance (EPR) spectrum of the binuclear CuA center in the water-soluble subunit II fragment from cytochrome ba3 of Thermus thermophilus was recorded at 3.93, 9.45, and 34.03 GHz, and the EPR parameters were determined by computer simulations. The frequency and M1 dependence of the linewidth was discussed in terms of g strain superimposed on a correlation between the A and g values. The g values were found to be gx = 1.996, gy = 2.011, gz = 2.187, and the two Cu ions contribute nearly equally to the hyperfine structure, with magnitude of Ax magnitude of approximately 15 G, magnitude of Ay magnitude = 29 G, and magnitude of Az magnitude of = 28.5 G (65Cu). Theoretical CNDO/S calculations, based on the x-ray structure of the Paracoccus denitrificans enzyme, yield a singly occupied antibonding orbital in which each Cu is pi*-bonded to one S and sigma*-bonded to the other. In contrast to the equal spin distribution suggested by the EPR simulations, the calculated contributions from the Cu ions differ by a factor of 2. However, only small changes in the ligand geometry are needed to reproduce the experimental results.
Department of Biochemistry and Biophysics, Göteborg University, Sweden. martin.karpefors@bcbp.gu.se
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M
Karpefors
C E
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Slutter
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JA
Fee
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Aasa
B
B
Källebring
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Larsson
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Vänngård
D001426:Bacterial Proteins / Q000737:chemistry*; D003300:Copper; D003573:Cytochrome b Group / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D003576:Electron Transport Complex IV / Q000737:chemistry*; D008667:Metalloproteins / Q000737:chemistry*; D016963:Thermus thermophilus / Q000737:chemistry*
D001426:Bacterial Proteins; D003573:Cytochrome b Group; D008667:Metalloproteins; D003300:Copper; C058557:cytochrome ba3; D003576:Electron Transport Complex IV