Observation of the Fe4+ = O stretching Raman band for cytochrome oxidase compound B at ambient temperature.
Resonance Raman and visible absorption spectra were simultaneously observed for cytochrome oxidase reaction intermediates at 5 degrees C by using the artificial cardiovascular system (Ogura, T., Yoshikawa, S., and Kitagawa, T. (1989) Biochemistry 28, 8022-8027) and a device for Raman/absorption simultaneous measurements (Ogura, T., and Kitagawa, T. (1988) Rev. Sci. Instrum. 59, 1316-1320). The Fe4+ = O stretching (nu FeO) Raman band was observed at 788 cm-1 for compound B for the first time. This band showed the 16O/18O isotopic frequency shift (delta nu FeO) by 40 cm-1, in agreement with that for horseradish peroxidase compound II (nu FeO = 787 cm-1 and delta nu FeO = 34 cm-1). In the time region when the FeII-O2 stretching band for compound A and the nu FeO band for compound B were coexistent, a Raman band assignable to the Fe3+-O-O-Cu2+ linkage was not recognized.
Ogura
T
T
Institute for Molecular Science, Okazaki National Research Institutes, Japan.
Takahashi
S
S
Shinzawa-Itoh
K
K
Yoshikawa
S
S
Kitagawa
T
T
D000818:Animals; D002417:Cattle; D003576:Electron Transport Complex IV / Q000302:isolation & purification / Q000378:metabolism*; D006735:Horseradish Peroxidase / Q000378:metabolism; D007501:Iron; D010100:Oxygen; D010103:Oxygen Isotopes; D013053:Spectrophotometry / Q000379:methods; D013059:Spectrum Analysis, Raman / Q000379:methods; D013816:Thermodynamics
D010103:Oxygen Isotopes; D007501:Iron; D006735:Horseradish Peroxidase; D003576:Electron Transport Complex IV; D010100:Oxygen