Resonance Raman detection of a v(Fe-CO) stretching frequency in cytochrome P-450scc from bovine adrenocortical mitochondria.
Resonance Raman scattering experiments on CO-complexed cytochrome P-450scc from bovine adrenocortical mitochondria demonstrate the simultaneous enhancement of v(Fe-CO) stretching and bound v(C-O) stretching frequencies at 477 and 1953 cm-1, respectively. These assignments were made on the basis of frequency shifts with the isotope 12C18O. This unusually low v(Fe-CO) stretching frequency in cytochrome P-450scc, compared with other CO-complexed hemoproteins such as CO-hemoglobin and -myoglobin, is presumably due to the thiolate ligation to the heme iron trans to CO and due to the linear and perpendicular configuration of CO binding to the heme.
D000302:Adrenal Cortex / Q000201:enzymology*; D000818:Animals; D002248:Carbon Monoxide; D002417:Cattle; D003577:Cytochrome P-450 Enzyme System; D006454:Hemoglobins; D007501:Iron; D008433:Mathematics; D008928:Mitochondria / Q000201:enzymology; D009211:Myoglobin; D013059:Spectrum Analysis, Raman
D006454:Hemoglobins; D009211:Myoglobin; D002248:Carbon Monoxide; D003577:Cytochrome P-450 Enzyme System; D007501:Iron