Resonance Raman assignment of myeloperoxidase and the selected mutants Asp94Val and Met243Thr. Effect of the heme distortion

Resonance Raman (RR) spectra have been acquired for human myeloperoxidase (MPO), and its Met243Thr and Asp94Val mutants with different excitation wavelengths and in polarized light. The proteins were characterized as ferric, ferrous and ferric–CN complexes in order to study the heme configuration in...

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Bibliographic Details
Published in:Journal of Raman spectroscopy 2006-01, Vol.37 (1-3), p.263-276
Main Authors: Brogioni, Silvia, Feis, Alessandro, Marzocchi, Mario P., Zederbauer, Martina, Furtmüller, Paul G., Obinger, Christian, Smulevich, Giulietta
Format: Article
Language:English
Subjects:
Bands
Covalence
Distortion
heme distortion
Human
Links
peroxidase
Proteins
resonance Raman spectroscopy
site-directed mutants
Spectra
symmetry-lowering
Wavelengths
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Summary:Resonance Raman (RR) spectra have been acquired for human myeloperoxidase (MPO), and its Met243Thr and Asp94Val mutants with different excitation wavelengths and in polarized light. The proteins were characterized as ferric, ferrous and ferric–CN complexes in order to study the heme configuration in various coordination, spin and oxidation states. Well‐defined spectra of the five‐coordinate high spin (ferrous), six‐coordinate high spin (ferric) and low spin (ferric–CN) species were obtained. The data allowed us to propose an almost complete assignment of the RR bands. The richness of the RR spectra of MPO is because of the activation of almost all the in‐plane skeletal modes observed for the Ni–octaethylporphyrin model compound, induced by the distortion of the heme imposed by the covalent links with the protein. The two mutants, which lost at least one of the covalent links between the protein and the heme group, were useful to determine the effect of the symmetry lowering of the heme group. Copyright © 2006 John Wiley & Sons, Ltd.
ISSN:0377-0486
1097-4555
DOI:10.1002/jrs.1442