Share Email Print

Proceedings Paper

Resonance Raman Spectroscopy Of Peroxidase Intermediates
Author(s): Andrew J. Sitter; Catherine M. Reczek; James Terner
Format Member Price Non-Member Price
PDF $14.40 $18.00
cover GOOD NEWS! Your organization subscribes to the SPIE Digital Library. You may be able to download this paper for free. Check Access

Paper Abstract

Resonance Raman spectroscopy has allowed the direct observation of the Fe(IV)=0 (oxo-ferryl) vibration in activated intermediates of heme enzymes. This mode is markedly sensitive to changes in the heme pocket environment. A study of variations among heme enzyme intermediates is beginning to provide a description of structure and dynamics in the active site during catalysis.

Paper Details

Date Published: 5 July 1989
PDF: 8 pages
Proc. SPIE 1055, Raman Scattering, Luminescence and Spectroscopic Instrumentation in Technology, (5 July 1989); doi: 10.1117/12.951598
Show Author Affiliations
Andrew J. Sitter, Virginia Commonwealth University (United States)
Catherine M. Reczek, Virginia Commonwealth University (United States)
James Terner, Virginia Commonwealth University (United States)

Published in SPIE Proceedings Vol. 1055:
Raman Scattering, Luminescence and Spectroscopic Instrumentation in Technology
Fran Adar; James E. Griffiths; Jeremy M. Lerner, Editor(s)

© SPIE. Terms of Use
Back to Top