Redox reaction of poly(ethylene oxide)-modified hemoglobin in poly(ethylene oxide) oligomers at 120 degrees C

Human hemoglobin, modified with poly(ethylene oxide) with average molecular weight of 3500 (PEO-Hb) was dissolved in PEO200 (molecular weight of 200) containing 0.5 M KCl. A quasi-reversible redox reaction of the PEO-Hb was found in PEO oligomers by alternatingly changing the potential polarity (+/- 1.2 V vs Ag). The PEO-Hb showed redox reactions in PEO200 even at 120 degrees C. PEO modification was concluded to give the thermal stability in some extent. In phosphate buffer at 70 degrees C, the electrochemical redox reaction of native Hb was not observed spectroscopically, but that of PEO-Hb was detected. The most effective factor was, however, concluded to be the use of PEO oligomers as a solvent. The molecular motion of PEO oligomers should be milder than that of water at higher temperature. This lower molecular motion was suggested to keep the redox activity of PEO-Hb in the PEO oligomer at 120 degrees C. However, the PEO-Hb in PEO200 was stable in the oxidized form at 30 degrees C; it was reduced without giving potential at 120 degrees C. Cyclic voltammetry revealed that this autoreduction was attributed to the shift of redox potential with elevating temperature.