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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.
S A Kretchmar, and
Z E Reyes, and
K N Raymond
April 1991,
Biochimica et biophysica acta,
S A Kretchmar, and
Z E Reyes, and
K N Raymond
May 1987,
Biochemical and biophysical research communications,
S A Kretchmar, and
Z E Reyes, and
K N Raymond
October 2003,
Acta crystallographica. Section D, Biological crystallography,
S A Kretchmar, and
Z E Reyes, and
K N Raymond
January 2012,
Biochemistry research international,
S A Kretchmar, and
Z E Reyes, and
K N Raymond
September 1982,
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S A Kretchmar, and
Z E Reyes, and
K N Raymond
December 2004,
Blood,
S A Kretchmar, and
Z E Reyes, and
K N Raymond
August 1983,
FEBS letters,
S A Kretchmar, and
Z E Reyes, and
K N Raymond
January 1981,
Proceedings of the National Academy of Sciences of the United States of America,
S A Kretchmar, and
Z E Reyes, and
K N Raymond
February 1988,
Biochimica et biophysica acta,
S A Kretchmar, and
Z E Reyes, and
K N Raymond
December 2009,
The protein journal,
