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Proceedings Paper

Structure and dynamics of the active site of peroxidases as revealed by resonance Raman spectroscopy
Author(s): G. Smulevich; A. M. English; Thomas G. Spiro
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Paper Abstract

Resonance Raman spectroscopy was used to probe the Fe axial ligation in cytochrome c peroxidase (CCP) its mutants and in horseradish peroxidase (HRP). The Fe-His stretching mode which was observed between 247 and 205 cn'' in the ferrous form of the CCP mutants was found to be a sensitive probe of imidazolate character of the proximal His-175 ligand of the Fe. In resting wild type CCP the Fe" atom is 5-coordinate high spin at neutral pH and room temperature. The RR investigations reveal that native CCP is delicately poised in this state since changes in pH temperature solvent composition or mutation of residues surrounding the heme can alter both the spin and coordination of the Fe" atom. RR studies on CCP single crystals show that the Fe" ligation behaviour mirrors that observed in solution. The Fe" ligation in resting HRP is also 5-coordinate high spin at room temperature. Lowering the temperature or addition of aromatic donor substrates also alters the state of the Fe" atom in IIRP. 1.

Paper Details

Date Published: 1 May 1991
PDF: 8 pages
Proc. SPIE 1403, Laser Applications in Life Sciences, (1 May 1991); doi: 10.1117/12.57323
Show Author Affiliations
G. Smulevich, Univ. di Firenze (Italy)
A. M. English, Concordia Univ. (Canada)
Thomas G. Spiro, Princeton Univ. (United States)


Published in SPIE Proceedings Vol. 1403:
Laser Applications in Life Sciences

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