The nature of the phosphate complex of sulphite oxidase from electron-paramagnetic-resonance studies

Biochem J. 1988 Nov 15;256(1):307-9. doi: 10.1042/bj2560307.

Abstract

The phosphate complex of sulphite oxidase in the Mo(V) oxidation state was investigated by e.p.r. spectroscopy. Third-derivative spectra reveal a wealth of structural detail previously unobserved in this spectrum. Most notable is the presence of hyperfine coupling from two inequivalent I = 1/2 nuclei, which we tentatively attribute to two 31P nuclei. Unresolved hyperfine interactions from at least one exchangeable 1H nucleus are also present.

MeSH terms

  • Electron Spin Resonance Spectroscopy
  • Macromolecular Substances
  • Oxidoreductases / metabolism*
  • Oxidoreductases Acting on Sulfur Group Donors / metabolism*
  • Phosphates / metabolism*

Substances

  • Macromolecular Substances
  • Phosphates
  • Oxidoreductases
  • Oxidoreductases Acting on Sulfur Group Donors