Electrochemical Properties of Protein Macromolecules and Their Active Groups

Electrochemical Properties of Protein Macromolecules and Their Active Groups 

The history of the use of electrochemical methods to study the properties of proteins, enzymes, and their component structural units is several decades old. Until quite recently, these studies were primarily associated with the use of polarography to solve analytical problems. The polarographic method of analysis has become very popular for determination of proteins, enzymes, and nucleic acids.It has been found that proteins irreversibly adsorb on mercury and in the presence of cobalt salts promote the evolution of hydrogen. In this case wave height is proportional to the amount of adsorbed protein. These studies have been summarized in some reviews and monographs.  

Much progress in the study of electrochemical properties of protein macromolecules has been achieved recently using another method, namely, the study of redox transformations of proteins, the carriers of electrons and enzymes, and their active groups at the electrode-electrolyte interface. This approach is intimately related to the use of enzymes to promote electrochemical reactions and pursues the purpose of elucidation of the mechanism of electron transport and the structural features of enzymes. 

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