| Abstract: | Spectroscopic studies have provided extensive information on the primary process of visual pigments and photoexcitation of chlorophyll as well as their effects on photoreactivity on the higher-order structures of protein has been observed only rarely. Resonance Raman spectroscopy can reveal the vibrational frequencies of the chromophore in a molecule provided the excitation wavelength is in the absorption band of that molecule. As the visible absorption bands of haemproteins are due to pi pi* transitions of the porphyrin ring, we can selectively observe the vibrational frequencies of iron porphyrin during in situ interactions with immediate amino acid residues of protein when the wavelength of excitation light is close to the Soret or Q band. Correlation of some vibrational frequencies of haem with the oxidation and spin states of the haem iron has been studied in detail and an empirical rules has been established. This method is therefore especially suitable for the study of an effect of higher-order structures of protein on the chromophore. We report here a photoreaction facilitated by a particular quaternary structure of protein--in various haemoglobins resonance Raman spectroscopy showed that reversible photoreduction of haem took place in the T state but not the R state. |
