Biological applications of resonance Raman spectroscopy: haem proteins

Abstract

Resonance Raman spectroscopy involves laser excitation within an absorption band of the sample. Certain vibrational modes, those which couple to the electronic transition, exhibit greatly increased Raman scattering in the resulting spectrum. Sensitivity approaches that of absorption spectrophotometry, while the high resolution characteristic of vibrational spectroscopy is preserved, even in solution at room temperature. If the resonant electronic transition is associated with a site of biological activity, then the technique offers a sensitive probe for structural features of the site. Haem proteins afford particularly informative resonance Raman spectra, with a rich assortment of porphyrin ring vibrations, which can be classified and analysed via their symmetry properties. Certain of these frequencies are sensitive to the structural concomitants of spin- and oxidation-state changes of the haem group. These can be used to monitor the structural consequences of ligation or electron transfer in haem proteins.