How resonance Raman spectroscopy can give valuable insights into diverse aspects of heme protein structure and function

Resonance Raman (RR) spectroscopy complemented by UV-Vis absorption spectroscopy is a very powerful technique to investigate the structure-function relationships of heme proteins, a widely distributed and biological relevant class of proteins which can play different biological functions. Since the protein activity is tightly linked to the structure of the heme active site, my study has been devoted to the investigation of several heme proteins involved in important biological processes, to obtain a comprehensive spectroscopic signature, with the aim to highlight the relationship between the heme pocket architecture and the protein function. The studies were carried out on native proteins and selected site-directed mutants, at both room (298 K) and low (80 K) temperature, at various pH, and in presence of various exogenous ligands, spanning the excitation wavelengths from UV to the visible region.