Abstract
This review provides examples illustrating the powerful combination of resonance Raman spectroscopy and site-directed mutagenesis to investigate the structure-function relationship in structurally different heme proteins with diverse physiological functionality. The selective mutation of key amino acid residues gives rise to distinct spectroscopic fingerprints, as a result of the subtle alterations of the heme pocket environment. This review includes, but it is not limited to, the study of: i) the interactions between bound exogenous ligands with distal residues, ii) the effects of hydrogen bonds between the proximal residues and the surrounding cavity, iii) the interaction between the peripheral substituents of the heme group with the protein matrix with the concomitant effect on specific biological processes.
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