51. Observation of 17O effects on MoV EPR spectra in sulfite oxidase; xanthine dehydrogenase, and MoO(SC6H5)4−
- Author
-
Stephen P. Cramer, Thomas N. Sorrell, Jean L. Johnson, and K.V. Rajagopalan
- Subjects
Coordination sphere ,Protein Conformation ,Xanthine Dehydrogenase ,Inorganic chemistry ,Biophysics ,chemistry.chemical_element ,Oxygen Isotopes ,Biochemistry ,Spectral line ,law.invention ,chemistry.chemical_compound ,law ,Sulfite oxidase ,Animals ,Oxidoreductases Acting on Sulfur Group Donors ,Electron paramagnetic resonance ,Molecular Biology ,Molybdenum ,chemistry.chemical_classification ,Chemistry ,Electron Spin Resonance Spectroscopy ,Oxygen ligand ,Ketone Oxidoreductases ,Cell Biology ,Enzyme ,Liver ,Xanthine dehydrogenase ,Oxidoreductases ,Chickens - Abstract
17 O effects have been observed on the Mo V EPR signals from sulfite oxidase, xanthine dehydrogenase, and MoO(SC 6 H 5 ) 4 − . The results point to the presence of a rapidly exchangeable oxygen ligand in the molybdenum coordination sphere of the enzymes. Average splittings were on the order of 10 gauss for the enzymes, but only about 2 gauss for MoO(SC 6 H 5 ) 4 − .
- Published
- 1979