Detection of vanadyl-nitrogen interaction in organs of the vanadyl-treated rat: electron spin echo envelope modulation study

AbstractESEEM spectroscopy was applied for the first time to organs of an animal, viz. the kidney and liver of the rat treated with vanadyl sulfate. The aim of this study is to investigate the in vivo coordination structure of vanadyl ions administrated, and to gain information concerning the insulin-mimic activity of vanadium. ESEEM measurements for kidney and liver performed at 77 K have established nitrogen coordination to a certain percentage of vanadyl ion in the organs. The rotios of nitrogen-coordinating vanadyl ion were estimated as 70–80% in the liver, and 50–55% in the kidney. Isotropic portions of the 14N HFC were estimated as |Aiso| ∼ 5.0 MHz for liver, and ∼ 5.2 MHz for kidney, indicating that the coordinating nitrogen is an amino nitrogen. Coordination of the Lys ϵ-amine or the N-terminal α-amine of a protein or (a peptide) to vanadyl ion in vivo is suggested

Characterization of neutrophil b-type cytochrome in situ by electron paramagnetic resonance spectroscopy

AbstractElectron paramagnetic resonance spectroscopy at 4.2 K was successfully used to characterize neutrophil b-type cytochrome in situ. The spectra or resting neutrophils taken under aerobic conditions gave a set of characteristic signals in a high magnetic field (g=2.85, 2.21 and 1.67) beside signals for myeloperoxidase and others. From the g values, shapes and the results of other experiments, these signals were attributed to those of cytochrome b558. The results indicate that cytochrome b558 in resting neutrophils is a hexa-coordinated ferric hemoprotein in a low-spin state. The obtained g??? and g??? values for the hemichrome were consistent with that of bis(imiduzole)-coordinated hemoprotein