Resonance Raman investigations of chloroperoxidase, horseradish peroxidase, and cytochrome c using Soret band laser excitation

Biochemistry
R D RembaL P Hager

Abstract

Resonance Raman spectra of the heme protein chloroperoxidase in its native and reduced forms and complexed with various small ions are obtained by using laser excitation in the Soret region (350-450 nm). Additionally, Raman spectra of horseradish peroxidase, cytochrome P-450cam, and cytochrome c, taken with Soret excitation, are presented and discussed. The data support previous findings that indicate a strong analogy between the active site environments of chloroperoxidase and cytochrome P-450cam. The Raman spectra of native chloroperoxidase are found to be sensitive to temperature and imply that a high leads to low spin transition of the heme iron atom takes place as the temperature is lowered. Unusual peak positions are also found for native and reduced chloroperoxidase and indicate a weakening of porphyrin ring bond strengths due to the presence of a strongly electron-donating axial ligand. Enormous selective enhancements of vibrational modes at 1360 and 674 cm-1 are also observed in some low-spin ferrous forms of the enzyme. These vibrational frequencies are assigned to primary normal modes of expansion of the prophyrin macrocycle upon electronic excitation.

References

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Citations

Jun 15, 1976·Biochemistry·G E KrejcarekL P Hager
Mar 16, 1977·Journal of the American Chemical Society·P M Champion, I C Gunsalus
Dec 2, 1975·Biochemistry·R H AustinI C Gunsalus
Apr 28, 1976·Journal of the American Chemical Society·L K HansonC R Connell
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Related Concepts

Ovoperoxidase
Alpha-Peroxidase
Raman Optical Activity Spectroscopy
Isocyanides
Horseradish allergenic extract
Cytochrome c Group
Plasma Protein Binding Capacity
Cytochromes
Porphyrins
Armoracia rusticana

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