Abstract
Cyclic voltammetry has been used to determine the reduction potentials of blue (Pseudomonas aeruginosa azurin) and purple (Thermus thermophilus CuA domain) copper proteins unfolded by guanidine hydrochloride. These Cu(II/I) potentials [456 (azurin); 453 (CuA) mV vs., NHE] are higher than those of the folded proteins. The downshift of the potential in the folded state can be accounted for by assuming that rack-induced axial coordination stabilizes Cu(II) relative to Cu(I) in a protein-encapsulated active site.
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Received: 3 March 1998 / Accepted: 6 April 1998
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Wittung-Stafshede, P., Hill, M., Gomez, E. et al. Reduction potentials of blue and purple copper proteins in their unfolded states: a closer look at rack-induced coordination. JBIC 3, 367–370 (1998). https://doi.org/10.1007/s007750050246
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DOI: https://doi.org/10.1007/s007750050246