Raman spectroscopic study of a non-heme iron enzyme soybean lipoxygenase - 1 in low hydrated media
Abstract This work is a contribution to the experimental study of the structure-function relationship of enzymes in non conventional media. As it is known that bound water play a determining role on affinity and specificity, we have chosen aqueous media with restricted water content. Water activity of the reaction media was decreased by addition of specific hydrosoluble cosolvents. Laser visible Raman spectroscopy was applied to determine the local (microenvironments of some aromatic residues) and global secondary and/or tertiary conformational changes of the model enzyme in the presence and absence of polyols or sugars at high concentrations.