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Electron paramagnetic resonance properties and oxidation-reduction potentials of the molybdenum, flavin, and iron-sulfur centers of chicken liver xanthine dehydrogenase.

Publication ,  Journal Article
Barber, MJ; Coughlan, MP; Kanda, M; Rajagopalan, KV
Published in: Arch Biochem Biophys
May 1980

Duke Scholars

Published In

Arch Biochem Biophys

DOI

ISSN

0003-9861

Publication Date

May 1980

Volume

201

Issue

2

Start / End Page

468 / 475

Location

United States

Related Subject Headings

  • Xanthine Dehydrogenase
  • Oxidation-Reduction
  • Molybdenum
  • Metalloproteins
  • Liver
  • Ketone Oxidoreductases
  • Iron-Sulfur Proteins
  • Hydrogen-Ion Concentration
  • Flavoproteins
  • Electron Spin Resonance Spectroscopy
 

Citation

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MLA
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Barber, M. J., Coughlan, M. P., Kanda, M., & Rajagopalan, K. V. (1980). Electron paramagnetic resonance properties and oxidation-reduction potentials of the molybdenum, flavin, and iron-sulfur centers of chicken liver xanthine dehydrogenase. Arch Biochem Biophys, 201(2), 468–475. https://doi.org/10.1016/0003-9861(80)90535-4
Barber, M. J., M. P. Coughlan, M. Kanda, and K. V. Rajagopalan. “Electron paramagnetic resonance properties and oxidation-reduction potentials of the molybdenum, flavin, and iron-sulfur centers of chicken liver xanthine dehydrogenase.Arch Biochem Biophys 201, no. 2 (May 1980): 468–75. https://doi.org/10.1016/0003-9861(80)90535-4.
Barber, M. J., et al. “Electron paramagnetic resonance properties and oxidation-reduction potentials of the molybdenum, flavin, and iron-sulfur centers of chicken liver xanthine dehydrogenase.Arch Biochem Biophys, vol. 201, no. 2, May 1980, pp. 468–75. Pubmed, doi:10.1016/0003-9861(80)90535-4.
Journal cover image

Published In

Arch Biochem Biophys

DOI

ISSN

0003-9861

Publication Date

May 1980

Volume

201

Issue

2

Start / End Page

468 / 475

Location

United States

Related Subject Headings

  • Xanthine Dehydrogenase
  • Oxidation-Reduction
  • Molybdenum
  • Metalloproteins
  • Liver
  • Ketone Oxidoreductases
  • Iron-Sulfur Proteins
  • Hydrogen-Ion Concentration
  • Flavoproteins
  • Electron Spin Resonance Spectroscopy