Abstract
Protein CopC from a pathogenic bacterium Pseudomonas syringae pv. tomato (CopC) is one of four proteins (CopA, B, C and D) coded on the copper resistance operon (cop). Using fluorescence measurements, differential optical spectra, methods of cyclic voltammetry and studing the kinetics of oxidation of ascorbic acid, we investigated the possibility of protein CopC binding with AuIII ion. The results showed that the AuIII ion can be bound with CopC in the ratio of 2: 1. The apparent binding constants k1 and k2 are 3.68·103 and 3.92·104 L mol−1, respectively. Binding with AuIII ions does not result in considerable conformational changes of protein CopC.
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