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Photodissociation of the CO Complex of Horseradish Peroxidase Studied by Laser-Induced Optoacoustic Spectroscopy
| Content Provider | Semantic Scholar |
|---|---|
| Author | Feis, Alessandro Angeloni, Leonardo |
| Copyright Year | 2001 |
| Abstract | Laser-induced optoacoustic spectroscopy (LIOAS) was applied to the study of the photolysis of the CO-ligated heme protein horseradish peroxidase isoenzyme C (HRP). Laser photolysis produced structural volume changes faster than 50 ns. The photoreaction volume and enthalpy changes were determined by means of temperature-dependent measurements in the range 6−23 °C. The volume change (+29.6 mL/mol) can be mainly attributed to the displacement of CO to the bulk solvent. The enthalpy change is mainly related to the Fe−C bond energy with little contribution from the protein matrix. The results are interpreted in terms of the structural properties of HRP, which has a direct exit channel from the heme to the solvent, and compared to related studies on the CO complexes with myoglobin and hemoglobin. |
| Starting Page | 2638 |
| Ending Page | 2643 |
| Page Count | 6 |
| File Format | PDF HTM / HTML |
| DOI | 10.1021/jp002639v |
| Volume Number | 105 |
| Alternate Webpage(s) | http://www.angleo.it/scieprof/lavori/48%20photodissociation.pdf |
| Alternate Webpage(s) | https://doi.org/10.1021/jp002639v |
| Language | English |
| Access Restriction | Open |
| Content Type | Text |
| Resource Type | Article |