Relationship between heme vinyl conformation and the protein matrix in peroxidases
Article first published online: 13 OCT 2003
Copyright © 2003 John Wiley & Sons, Ltd.
Journal of Raman Spectroscopy
Volume 34, Issue 10, pages 725–736, October 2003
How to Cite
Marzocchi, M. P. and Smulevich, G. (2003), Relationship between heme vinyl conformation and the protein matrix in peroxidases. J. Raman Spectrosc., 34: 725–736. doi: 10.1002/jrs.1037
- Issue published online: 13 OCT 2003
- Article first published online: 13 OCT 2003
- Manuscript Accepted: 7 MAY 2003
- Manuscript Received: 10 FEB 2003
- Italian National Council of Research (CNR).
- Italian Ministry of Education, Universities and Research.
- vinyl orientation;
- electronic conjugation;
A direct relationship between the ν and Cb atoms of the vinyl groups and the surrounding atoms, the origin of the different vinyl orientations is ascribed to a variety of interactions, namely van der Waals contacts, weak π–π electron interactions and C—H···O hydrogen bonds. The vinyl group orientations appear to depend on the concerted orientations of the distal helix B and proximal helix F axes as controlled by the H-bonds between the distal Arg, a heme propionyl group and a residue on the extended strand adjacent to proximal helix F. Finally, a possible mechanism explaining the alkaline configuration changes of cytochrome c peroxidase and the reorientation of a vinyl group upon fluoride complexation is given. Copyright © 2003 John Wiley & Sons, Ltd.