Abstract
The binding of vanadyl to a porcine and bovine testicular S-100-like protein and to calmodulin was demonstrated using X-band (9.2 gHz) electron paramagnetic resonance (EPR) spectroscopy in aqueous solution at pH 7.4. In liquid solutions at 22°C, the vanadyl-protein complexes yielded VO2+ near rigid limit spectra. At 122 K, each of the three high-field resonances (i.e., 3/2, 5/2, and 7/2 parallel components) splits into two components indicating the presence of two classes of vanadyl-binding sites in each protein. The spectra of the frozen solutions were simulated to give parallel and perpendicular components of the hyperfine coupling constant and g factors similar to other vanadyl-protein complexes.
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Ahmed, R.H., Nieves, J., Kim, L. et al. Vanadyl binding to a testicular S-100-like protein and to calmodulin: Electron paramagnetic resonance spectra of VO2+-protein complexes. J Protein Chem 6, 431–439 (1987). https://doi.org/10.1007/BF02343340
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DOI: https://doi.org/10.1007/BF02343340