Effect of low temperature on soybean peroxidase: spectroscopic characterization of the quantum-mechanically admixed spin state
| Autor: | Chiara Indiani, Alessandro Feis, Barry D Howes, Mario P Marzocchi, Giulietta Smulevich |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Porphyrins
Spin states Protein Conformation Analytical chemistry Heme Spectrum Analysis Raman Biochemistry law.invention Inorganic Chemistry chemistry.chemical_compound symbols.namesake law Freezing Spin (physics) Electron paramagnetic resonance Spectroscopy Binding Sites Electron Spin Resonance Spectroscopy Imidazoles Resonance Porphyrin Recombinant Proteins Crystallography Peroxidases chemistry Spectrophotometry symbols Quantum Theory Thermodynamics Soybeans Raman spectroscopy |
| Zdroj: | Journal of Inorganic Biochemistry. 79:269-274 |
| ISSN: | 0162-0134 |
| DOI: | 10.1016/s0162-0134(99)00156-7 |
| Popis: | A spectroscopic study of soybean peroxidase (SBP) has been carried out using electronic absorption, resonance Raman (RR) and electron paramagnetic resonance (EPR) spectroscopy in order to determine the effects of temperature on the heme spin state. Upon lowering the temperature a transition from high spin to low spin is induced in SBP resulting from conformational changes in the heme cavity, including a contraction of the heme core, the reorientation of the vinyl group in position 2 of the porphyrin macrocycle, and the binding of the distal His to the Fe atom. Moreover, the combined analysis of the data derived from the different techniques at both room and low temperatures demonstrates that at low temperature the quantum-mechanically admixed spin state (QS) of SBP has RR frequencies different from those observed for the QS species at room temperature. |
| Databáze: | OpenAIRE |
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