14N-coordination to VO 2+in reduced vanadium bromoperoxidase, an electron spin echo study

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