Folding degrees of azurins and pseudoazurins

• Published in: Computational biology and chemistry Vol. 29; no. 5; pp. 345 - 353
• Main Authors: Estrada, Ernesto, Uriarte, Eugenio
• Format: Journal Article
• Language: English
• Published: Elsevier Ltd 01.10.2005
• Subjects: Blue copper proteins; Copper binding site; Folding degree; Protein geometry; Structure–function relation; Blue copper proteins; Structure–function relation; Folding degree; Protein geometry; Copper binding site
• ISSN: 1476-9271; 1476-928X
• DOI: 10.1016/j.compbiolchem.2005.06.005

A quantitative measure of the degree of folding of azurins and pseudoazurins has been made. We have found that the reduction potential of azurins and pseudoazurins is a function of the contribution to the degree of folding of His117, a key amino acid in electron transfer which is directly bonded to copper in these proteins. The folding degree of His117 explains 95% of the variance in the experimental values of the reduction potential of azurins and pseudoazurins. The change in the folding degree of this amino acid influences several geometric parameters of the main backbones of these proteins. Among them, the angle formed between N(His117)⋯Cu⋯S(Cys112), which plays an important role in electron transport, but not the N(His117)⋯Cu distance, shows some non-linear correlation with the reduction potential of azurins and pseudoazurins. However, it is only able to explain less than 75% in the variance of the reduction potential of these proteins instead of the 95% explained by the folding degree of His117.