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Updated: Aug 3, 2025

A Novel Technique for Raman Analysis of Highly Radioactive Samples Using Any Standard Micro-Raman Spectrometer
Published on: April 12, 2017
Resonance Raman Characterization of O2-Binding Heme Proteins
Samuel N Snyder1, Tapiwa Chiura1, Piotr J Mak2
1Department of Chemistry, Saint Louis University, Saint Louis, MO, USA.
Abstract:
A vast array of critical in vivo processes and pathways are dependent on a multitude of O2-binding heme proteins which contain a diverse range of functions. Resonance Raman (rR) spectroscopy is an ideal technique for structural investigation of these proteins, providing information about the geometry of the Fe-O-O fragment and its electrostatic interactions with the distal active site. Characterization of these oxy adducts is an endeavor that is complicated by their instability for many heme proteins in solution, an obstacle which can be overcome by applying the rR technique to cryogenically frozen samples. We describe here how to measure rR spectra of heme proteins with stable oxy forms, as well as the technical adaptations required to measure unstable samples at 77 K.
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