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- W4206265562 abstract "The endogenous cation in peroxidases may contribute to the type of heme coordination. Here a series of ferric and ferrous derivatives of wild-type Leishmania major peroxidase (LmP) and of engineered K+ site mutants of LmP, lacking potassium cation binding site, has been examined by electronic absorption spectroscopy at 25 °C. Using UV–visible spectrophotometry, we show that the removal of K+ binding site causes substantial changes in spin states of both the ferric and ferrous forms. The spectral changes are interpreted to be, most likely, due to the formation of a bis-histidine coordination structure in both the ferric and ferrous oxidation states at neutral pH 7.0. Stopped flow spectrophotometric techniques revealed that characteristics of Compound I were not observed in the K+ site double mutants in the presence of H2O2. Similarly electron donor oxidation rate was two orders less for the K+ site double mutants compared to the wild type. These data show that K+ functions in preserving the protein structure in the heme surroundings as well as the spin state of the heme iron, in favor of the enzymatically active form of LmP." @default.
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- W4206265562 date "2021-11-01" @default.
- W4206265562 modified "2023-10-16" @default.
- W4206265562 title "Lingual Mucocutaneous Leishmaniasis" @default.
- W4206265562 doi "https://doi.org/10.1016/j.otoeng.2021.02.001" @default.
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