Resonance Raman Spectroscopy Of Peroxidase Intermediates

Andrew J. Sitter; Catherine M. Reczek; James Terner

doi:10.1117/12.951598

5 July 1989 Resonance Raman Spectroscopy Of Peroxidase Intermediates

Andrew J. Sitter, Catherine M. Reczek, James Terner

Proceedings Volume 1055, Raman Scattering, Luminescence and Spectroscopic Instrumentation in Technology; (1989) https://doi.org/10.1117/12.951598
Event: OE/LASE '89, 1989, Los Angeles, CA, United States

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.

Citation Download Citation

Andrew J. Sitter, Catherine M. Reczek, and James Terner "Resonance Raman Spectroscopy Of Peroxidase Intermediates", Proc. SPIE 1055, Raman Scattering, Luminescence and Spectroscopic Instrumentation in Technology, (5 July 1989); https://doi.org/10.1117/12.951598

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