Resonance Raman enhancement of phenyl ring vibrational modes in phenyl iron complex of myoglobin.
Resonance Raman spectra are reported for the organometallic phenyl-FeIII complexes of horse heart myoglobin. We observed the resonance enhancement of the ring vibrational modes of the bound phenyl group. They were identified at 642, 996, 1,009, and 1,048 cm-1, which shift to 619, 961, 972, and 1,030 cm-1, respectively, upon phenyl 13C substitution. The lines at 642 and 996 cm-1 are assigned, respectively, as in-plane phenyl ring deformation mode (derived from benzene vibration No. 6a at 606 cm-1) and out-of-plane CH deformation (derived from benzene vibration No. 5 at 995 cm-1). The frequencies of the ring "breathing" modes at 1,009 and 1,048 cm-1 are higher than the corresponding ones in phenylalanine (at 1,004 and 1,033 cm-1) and benzene (at 992 and 1,010 cm-1), indicating that the ring C--C bonds are strengthened (or shortened) when coordinated to the heme iron. The excitation profiles of these phenyl ring modes and a porphyrin ring vibrational mode at 674 cm-1 exhibit peaks near its Soret absorption maximum at 431 nm. This appears to indicate that these phenyl ring modes may be enhanced via resonance with the Soret pi-pi transition. The FeIII--C bond stretching vibration has not been detected with excitation wavelengths in the 406.7-457.9-nm region.
Liu
H H
HH
School of Chemistry, Georgia Institute of Technology, Atlanta 30332.
Lin
S H
SH
Yu
N T
NT
D000818:Animals; D002247:Carbon Isotopes; D006418:Heme / Q000378:metabolism; D006736:Horses; D007501:Iron / Q000378:metabolism*; D007553:Isotope Labeling / Q000379:methods; D009206:Myocardium / Q000378:metabolism; D009211:Myoglobin / Q000378:metabolism*; D010659:Phenylhydrazines / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D013059:Spectrum Analysis, Raman / Q000379:methods; D014732:Vibration
D002247:Carbon Isotopes; D009211:Myoglobin; D010659:Phenylhydrazines; C030299:phenylhydrazine; D006418:Heme; D007501:Iron