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