The spectroelectrochemical determination of the reduction potential of diferric serum transferrin.

The first spectroelectrochemical measurement of the formal reduction potential of iron transferrin has been carried out using methyl viologen to mediate electron transfer to the protein. These calculations take into consideration the weak nature of the ferrous transferrin complex. A value of -0.52(8) V vs. the normal hydrogen electrode was obtained in 0.100 M tris(hydroxymethyl)aminomethane buffer at pH 7.4, 22 degrees C, and 2.0 M KCl. A high ionic strength was necessary to effect reduction, supporting the observation that ions play an important role in the reduction of iron in transferrin. Finally, a procedure for carrying out the reduction of methyl viologen at a gold electrode in a spectrophotometric cell is described.