The nature of the phosphate complex of sulphite oxidase from electron-paramagnetic-resonance studies.
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.
George
G N
GN
Exxon Research and Engineering, Annandale, NJ.
Prince
R C
RC
Kipke
C A
CA
Sunde
R A
RA
Enemark
J H
JH
D004578:Electron Spin Resonance Spectroscopy; D046911:Macromolecular Substances; D010088:Oxidoreductases / Q000378:metabolism*; D050862:Oxidoreductases Acting on Sulfur Group Donors / Q000378:metabolism*; D010710:Phosphates / Q000378:metabolism*
D046911:Macromolecular Substances; D010710:Phosphates; D010088:Oxidoreductases; D050862:Oxidoreductases Acting on Sulfur Group Donors