ABSTRACT
The application of resonance Raman (RR) spectroscopy to the investigation of biological chromophores, typically the focus of chemical reactivity and interest, is becoming increasingly widespread. This technique is highly structure sensitive because the frequencies of specific bond vibrations of such chromophores are observable, free from interference by the bulk of the sample. The analysis of the location, shapes, and intensities of the observed peaks contained in a Raman spectrum, and in the case of RR spectroscopy, in a series of excitation wavelength-dependent spectra, will yield both molecular and electronic structural details of the system under investigation. The nonblue designation refers to Cu(II) centers in proteins with Electron paramagnetic resonance and electronic absorption properties characteristic of copper in inorganic complexes. RR spectroscopy has proved to be a useful technique for obtaining direct information on the nature of copper ligands and coordination geometry in copper proteins.
