Autor: |
de Boer, Eize, Keijzers, Cornelus P., Klaassen, Adri A.K., Reijerse, Eduard J., Collison, David, Garner, C.David, Wever, Ron |
Zdroj: |
FEBS Letters; January 1988, Vol. 235 Issue: 1 p93-97, 5p |
Abstrakt: |
Vanadium bromoperoxidase from the brown seaweed Ascophyllum nodosumwas studied with electron spin echo envelope modulation (ESEEM) spectroscopy. After comparing the Fourier transformed (FT) ESEEM spectra with those of a number of vanadyl model compounds, it could be concluded that nitrogen is present in the equatorial plane of the vanadyl cation of reduced bromoperoxidase ( 14N frequencies occurred at 3.1, 4.2, 5.3 and 8.1 MHz). Furthermore, the FT-ESEEM spectra of reduced bromoperoxidase exhibited an intense 1H modulation (13.8 MHz), which was completely replaced by a deuterium modulation at ∼2 MHz when bromoperoxidase was dissolved in D 2O, instead of H 2O. These latter data confirm earlier EPR experiments on reduced bromoperoxidase [(1988) Biochemistry 27, 1629–1635], showing that the oxo-vanadium (IV) ion is coupled to exchangeable protons. |
Databáze: |
Supplemental Index |
Externí odkaz: |
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