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Optical spectra of lactoperoxidase as a function of solvent
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Umeå University, Faculty of Science and Technology, Umeå Plant Science Centre (UPSC).
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2005 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 44, no 48, 15953-15959 p.Article in journal (Refereed) Published
Abstract [en]

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 shows a solvent-dependent transition; the high-spin form is predominant in anhydrous sugar glass, but in the presence of water, the low-spin form is also present in abundance. The active site of lactoperoxidase is not as tightly constrained at low pH as at neutrality, though the enzyme is active over a wide pH range.

Place, publisher, year, edition, pages
Washington: American Chemical Society (ACS), 2005. Vol. 44, no 48, 15953-15959 p.
Keyword [en]
molecular-dynamics simulations, infrared spectroscopy, absorption-spectroscopy, prosthetic group, resonance raman, heme-proteins, active site, peroxidase, myeloperoxidase, binding
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-18882DOI: 10.1021/bi0513655ISI: 000233704900034PubMedID: 16313199OAI: oai:DiVA.org:umu-18882DiVA: diva2:175014
Available from: 2009-02-26 Created: 2009-02-26 Last updated: 2017-12-13Bibliographically approved

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