Spectroscopic characterization and electrochemistry of poly(ethylene oxide)-modified myoglobin in organic solvents.
Myoglobin (Mb) was chemically modified with activated poly(ethylene oxide) (PEO) (average molecular weight of 2000) to solubilize it in various organic solvents. UV-vis, circular dichroism, and Raman spectroscopy were used to characterize the structure correlated with the electron-transfer reactions of PEO-modified Mb (PEO-Mb). Spectroscopic data indicated changes in heme coordination geometry for PEO-Mb in various organic solvents that are different from that in water. The Raman spectrum showed the characteristics of PEO-Mb in PEO oligomer (average MW of 200) in the five-coordinate high-spin state, which facilitates fast electron-transfer reactions between protein and the glassy carbon electrode. These results suggest heme environment effects on the properties of proteins in organic solvents.
Wiwatchaiwong
Supranee
S
Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Koganei, Tokyo 184-8588, Japan.
Nakamura
Nobuhumi
N
Ohno
Hiroyuki
H
D000818:Animals; D001709:Biotechnology / Q000379:methods*; D002625:Chemistry, Organic / Q000379:methods*; D002942:Circular Dichroism; D004563:Electrochemistry / Q000379:methods*; D006736:Horses; D008956:Models, Chemical; D018482:Muscle, Skeletal / Q000378:metabolism; D009211:Myoglobin / Q000378:metabolism*; D011092:Polyethylene Glycols / Q000737:chemistry*; D012997:Solvents / Q000737:chemistry*; D013053:Spectrophotometry / Q000379:methods*; D013056:Spectrophotometry, Ultraviolet; D013059:Spectrum Analysis, Raman
D009211:Myoglobin; D012997:Solvents; D011092:Polyethylene Glycols