Presented as part of a commemorative issue for Wolfgang Kiefer on the occasion of his 65th birthday.
Resonance Raman assignment of myeloperoxidase and the selected mutants Asp94Val and Met243Thr. Effect of the heme distortion†
Article first published online: 12 JAN 2006
Copyright © 2006 John Wiley & Sons, Ltd.
Journal of Raman Spectroscopy
Special Issue: Commemorative Issue: for Wolfgang Kiefer on the Occasion of his 65th Birthday
Volume 37, Issue 1-3, pages 263–276, January - March 2006
How to Cite
Brogioni, S., Feis, A., Marzocchi, M. P., Zederbauer, M., Furtmüller, P. G., Obinger, C. and Smulevich, G. (2006), Resonance Raman assignment of myeloperoxidase and the selected mutants Asp94Val and Met243Thr. Effect of the heme distortion. J. Raman Spectrosc., 37: 263–276. doi: 10.1002/jrs.1442
- Issue published online: 12 JAN 2006
- Article first published online: 12 JAN 2006
- Manuscript Accepted: 25 JUL 2005
- Manuscript Received: 2 MAY 2005
- Università di Firenze.
- Austrian Science Fund. Grant Number: (Project P15660).
- resonance Raman spectroscopy;
- heme distortion;
- site-directed mutants;
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.