14N‐coordination to VO2+ in reduced vanadium bromoperoxidase, an electron spin echo study

Vanadium bromoperoxidase from the brown seaweed Ascophyllum nodosum was 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 prese...

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Bibliographic Details
Published in:FEBS letters 1988-08, Vol.235 (1-2), p.93-97
Main Authors: de Boer, Eize, Keijzers, Cornelus P., Klaassen, Adri A.K., Reijerse, Eduard J., Collison, David, Garner, C.David, Wever, Ron
Format: Article
Language:English
Subjects:
Ascophyllum nodosum
Biological and medical sciences
Bromoperoxidase
ESEEM
Fundamental and applied biological sciences. Psychology
Molecular biophysics
Spectroscopy : techniques and spectras
Vanadium
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Summary:Vanadium bromoperoxidase from the brown seaweed Ascophyllum nodosum was 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 D2O, instead of H2O. 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.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(88)81240-7