Effect of alcohol on exercise-induced changes in serum glucose and serum free fatty acids |
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Authors: | E Heikkonen R Ylikahri R Roine M V?lim?ki M H?rk?nen M Salaspuro |
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Affiliation: | Beckman Institute, California Institute of Technology, Pasadena, CA 91125, USA. pernilla@cco.caltech.edu |
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Abstract: | Electrochemical measurements show that there are high-potential states of two copper proteins, Pseudomonas aeruginosa azurin and Thermus thermophilus CuA domain; these perturbed states are formed in guanidine hydrochloride (GuHCl) solution in which the proteins are still blue (azurin) and purple (CuA). In each case, the high-potential state forms reversibly. Absorption (azurin, CuA), visible circular dichroism (azurin, CuA), resonance-Raman (CuA), and EPR (CuA) spectra indicate that the structure of the oxidized copper site of each high-potential form is very similar to that of the native protein. It is proposed that GuHCl perturbs one or more H-bonds in the blue or purple copper active site, thereby allowing Cu(I) to adopt a more favorable coordination structure than that in the rigid cavity of the native protein. |
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