Abstract:
: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.
journal_name
Biochem Soc Transjournal_title
Biochemical Society transactionsauthors
Ingledew WJ,Rich PRdoi
10.1042/BST0330886keywords:
subject
Has Abstractpub_date
2005-08-01 00:00:00pages
886-9issue
Pt 4eissn
0300-5127issn
1470-8752pii
BST0330886journal_volume
33pub_type
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