Red-excitation resonance Raman analysis of the nu(Fe=O) mode of ferryl-oxo hemoproteins.
The Raman excitation profile of the nuFe O mode of horseradish peroxidase compound II exhibits a maximum at 580 nm. This maximum is located within an absorption band with a shoulder assignable to an oxygen-to-iron charge transfer band on the longer wavelength side of the alpha-band. Resonance Raman bands of the nuFe O mode of various ferryl-oxo type hemoproteins measured at 590 nm excitation indicate that many hemoproteins in the ferryl-oxo state have an oxygen-to-iron charge transfer band in the visible region. Since this red-excited resonance Raman technique causes much less photochemical damage in the proteins relative to blue-excited resonance Raman spectroscopy, it produces a higher signal-to-noise ratio and thus represents a powerful tool for investigations of ferryl-oxo intermediates of hemoproteins.
Department of Life Science, Graduate School of Life Science, University of Hyogo, Hyogo, Japan.
Kenichiro
K
Ikemura
Masahiro
M
Mukai
Hideo
H
Shimada
Tomitake
T
Tsukihara
Satoru
S
Yamaguchi
Kyoko
K
Shinzawa-Itoh
Shinya
S
Yoshikawa
Takashi
T
Ogura
D006420:Hemeproteins / Q000737:chemistry*; D006735:Horseradish Peroxidase / Q000737:chemistry*; D007501:Iron / Q000737:chemistry*; D010100:Oxygen / Q000737:chemistry*; D013059:Spectrum Analysis, Raman / Q000379:methods*
D006420:Hemeproteins; C066317:ferryl iron; D007501:Iron; D006735:Horseradish Peroxidase; D010100:Oxygen