The subtractively normalized interfacial Fourier transform infrared spectro
scopy (SNIFTIRS) has been used to examine an oxidation product from adsorpt
ion of the enzyme, ribonuclease A, at the platinum electrode. At potentials
of 600 mV (SCE), a negative going peak due to the formation of the oxidati
on product CO2 was clearly visible with both s- and p-polarized IR beams. T
his gives evidence that adsorption of the protein occurs through the carbox
ylate groups of the acidic residues of the protein at anodic potentials wit
h subsequent oxidation occurring by a decarboxylation mechanism. (C) 2000 A
cademic Press.