Abstract
The electrochemical behavior of cytochrome c (cyt- c) adsorbed to gold electrodes through mercaptoalkanoic acid/mercaptoalcohol monolayers was investigated in the 1-butyl-3-methylimidazolium salts of bis(trifluoromethylsulfonyl)imide and hexafluorophosphate. Cyt- c does not retain its Fe(III)/Fe(II) redox activity in dry ionic liquids (ILs); however, the redox signal of the modified electrodes can be reconstituted upon subsequent treatment with aqueous buffer. Water saturated ILs, 1.4 wt.%, failed to support the redox activity of the adsorbed cyt- c; therefore, the ILs’ deleterious effects on the redox behavior of the cyt- c modified electrodes cannot be attributed solely to the stripping of essential water from the enzyme's polypeptide lattice.
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