The combination of resonance Raman spectroscopy and site directed mutagenesis to study the diverse aspects of heme protein structure and function

被引:2
作者
Sebastiani, Federico [1 ]
Dali, Andrea [1 ]
Smulevich, Giulietta [1 ]
机构
[1] Dipartimento Chim Ugo Schiff DICUS, via Lastruccia 3-13, I-50019 Sesto Fiorentino, FI, Italy
关键词
resonance Raman; structure-function relationship; vibrational signatures; ligands; substituents groups; key residues; CYTOCHROME-C PEROXIDASE; TRUNCATED HEMOGLOBIN-O; MYCOBACTERIUM-TUBERCULOSIS; ELECTRONIC-ABSORPTION; LIGAND-BINDING; CATALASE-PEROXIDASE; HYDROGEN-PEROXIDE; SINGLE-CRYSTALS; SPECTRA; COPROHEME;
D O I
10.1142/S1088424622300026
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
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.
引用
收藏
页码:755 / 764
页数:10
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