Optical spectra of lactoperoxidase as a function of solvent
Yazarlar (6)
| Makale Türü | Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale) | ||
| Dergi Adı | Biochemistry (Q2) | ||
| Dergi ISSN | 0006-2960 Dergi Bilgileri (2005) | ||
| Makale Dili | – | Basım Tarihi | 12-2005 |
| Kabul Tarihi | – | Yayınlanma Tarihi | 08-11-2005 |
| Cilt / Sayı / Sayfa | 44 / 48 / 15953–15959 | DOI | 10.1021/bi0513655 |
| Makale Linki | https://pubs.acs.org/doi/abs/10.1021/bi0513655 | ||
| UAK Araştırma Alanları |
Dedektör Teknolojisi
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| Özet |
| The iron of lactoperoxidase is predominantly high-spin at ambient temperature. Optical spectra of lactoperoxidase indicate that the iron changes from high-spin to low-spin in the temperature range from room temperature to 20 K. The transformation is independent of whether the enzyme is in glycerol/water or solid sugar glass. Addition of the inhibitor benzohydroxamic acid increases the amount of the low-spin form, and again the transformation is independent of whether the protein is in an aqueous solution or a nearly anhydrous sugar. In contrast to lactoperoxidase, horseradish peroxidase remains high-spin over the temperature excursion in both solvents and with addition of benzohydroxamic acid. We conclude that details of the heme pocket of lactoperoxidase allow ligation changes with temperature that are dependent upon the apoprotein but independent of solvent fluctuations. At low pH, lactoperoxidase … |
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| Google Scholar | 9 |