A study of the horseradish peroxidase catalytic site by FTIR spectroscopy
| Autor: | W. J. Ingledew, Peter R. Rich |
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| Rok vydání: | 2005 |
| Předmět: |
Models
Molecular chemistry.chemical_classification Photolysis biology Ligand Circular Dichroism Infrared spectroscopy Heme Photochemistry Biochemistry Horseradish peroxidase Armoracia Catalysis Amino acid chemistry Catalytic Domain Spectroscopy Fourier Transform Infrared biology.protein Peptide bond sense organs Fourier transform infrared spectroscopy Spectroscopy Horseradish Peroxidase Plant Proteins |
| Zdroj: | Biochemical Society Transactions. 33:886-889 |
| ISSN: | 1470-8752 0300-5127 |
| DOI: | 10.1042/bst0330886 |
| Popis: | Vibrational changes in the catalytic site of horseradish peroxidase were investigated by FTIR (Fourier-transform infrared) spectroscopy in the 1000–2500 cm−1 range. Difference spectra were generated by photolysis of the haemII-CO compound at different pH/pD values. The spectra report on the fine structure around the catalytic site and show vibrational changes of protein backbone, amino acid residues and cofactors. Assignments of the FTIR vibrations can be made based upon known crystal structures, comparisons with absorption frequencies and extinction coefficients of model amino acids and cofactors, effects of H2O/2H2O exchange and changes of pH/pD. Concomitant with the photolysis of the CO ligand are changes due to haem and protein vibrations, predominant among which are arginine and histidine residue vibrations. |
| Databáze: | OpenAIRE |
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