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

FEBS Letters

de Boer, Eize¹  Klaassen, Adri A.K.²  Wever, Ron¹  Reijerse, Eduard J.²  Garner, C.David³  Collison, David³  Keijzers, Cornelus P.¹ 

[1] Laboratory of Biochemistry, University of Amsterdam, PO Box 20151, 1000 HD Amsterdam, The Netherlands;Department of Molecular Spectroscopy, University of Nijmegen, Toernooiveld, 6525 ED Nijmegen, The Netherlands;Chemistry Department, University of Manchester, Manchester M13 9PL, England

关键词: Vanadium;    Bromoperoxidase;    ESEEM;    (Ascophyllum nodosum);   

DOI  :  10.1016/0014-5793(88)81240-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown