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

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.

[1]  Teizo Kitagawa,et al.  Resonance Raman spectra of octaethylporphyrinato‐Ni(II) and meso‐deuterated and 15N substituted derivatives. I. Observation and assignments of nonfundamental Raman lines , 1978 .

[2]  Y. Kyōgoku,et al.  Resonance Raman spectra of octaethylporphyrinato‐Ni(II) and meso‐deuterated and 15N substituted derivatives. II. A normal coordinate analysis , 1978 .

[3]  P. Champion,et al.  Resonance Raman investigations of cytochrome P450CAM from Pseudomonas putida , 1978 .

[4]  Y. Kyōgoku,et al.  Resonance Raman spectra of 15N enriched metallooctaethylorphyrins. Characterization of the oxidation state marker bands of hemoproteins , 1977 .

[5]  P. Champion,et al.  Resonance Raman spectra of cytochrome P450cam. , 1977, Journal of the American Chemical Society.

[6]  A. Lewis,et al.  Continuously tunable optical filter for use in resonance Raman spectroscopy. , 1977, Applied optics.

[7]  H. Bernstein,et al.  The vibrational spectra of the metalloporphins: A normal coordinate analysis of the planar vibrations in the Cu‐chelates of porphin, porphin‐d4 (meso), 1:3:5:7‐tetramethyl porphin and 1:2:3:4:5:6:7:8‐octamethyl porphin , 1976 .

[8]  Y. Ozaki,et al.  An anomaly in the resonance Raman spectra of cytochrome P-450cam in the ferrous high-spin state. , 1976, Journal of biochemistry.

[9]  L. Hager,et al.  Oxidation-reduction potential measurements on chloroperoxidase and its complexes. , 1976, Biochemistry.

[10]  R. Hochstrasser,et al.  Approximate selection rules for resonance Raman spectroscopy , 1976 .

[11]  R. Bryant,et al.  Broad-line nuclear magnetic resonance studies of chloroperoxidase. , 1976, Biochemistry.

[12]  C. Djerassi,et al.  Letter: Chloroperoxidase. Evidence for P-450 type heme environment from magnetic circular dichroism spectroscopy. , 1976, Journal of the American Chemical Society.

[13]  C. R. Connell,et al.  Letter: Origin of the anomalous Soret spectra of carboxycytochrome P-450. , 1976, Journal of the American Chemical Society.

[14]  H Frauenfelder,et al.  Dynamics of ligand binding to myoglobin. , 1975, Biochemistry.

[15]  P. Champion,et al.  Mössbauer investigations of high-spin ferrous heme proteins. II. Chloroperoxidase, horseradish peroxidase, and hemoglobin. , 1975, Biochemistry.

[16]  P. Stein,et al.  STRUCTURAL INTERPRETATION OF HEME PROTEIN RESONANCE RAMAN FREQUENCIES, PRELIMINARY NORMAL COORDINATE ANALYSIS RESULTS , 1975 .

[17]  T. Spiro,et al.  Resonance Raman spectra of horseradish peroxidase: evidence for anomalous heme structure. , 1974, Biochemistry.

[18]  A. Lewis,et al.  Resonant Raman scattering from cytochrome c: Frequency dependence of the depolarization ratio , 1973 .

[19]  R. Hochstrasser,et al.  A description of resonant raman scattering ln hemeproteins: Cytochrome-c , 1973 .

[20]  P. Champion,et al.  Mössbauer investigations of chloroperoxidase and its halide complexes. , 1973, Biochemistry.

[21]  D. Morris,et al.  Chloroperoxidase. VII. Classical peroxidatic, catalatic, and halogenating forms of the enzyme. , 1970, The Journal of biological chemistry.

[22]  J. L. Smith,et al.  The Oxygen Tension of Arterial Blood , 1896, The Journal of physiology.