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Selenite binding to carbon monoxide oxidase from Pseudomonas carboxydovorans. Selenium binds covalently to the protein and activates specifically the CO----methylene blue reaction.

Publication ,  Journal Article
Meyer, O; Rajagopalan, KV
Published in: J Biol Chem
May 10, 1984

The CO----methylene blue and CO----dichlorophenol indophenol activities of carbon monoxide oxidase were specifically activated upon aerobic incubation with selenite, whereas the NADH----methylene blue activity was not altered. Fully active enzyme contained selenium, molybdenum, and flavin adenine dinucleotide in a 1:1:1 ratio. Selenium was covalently bound to the protein, probably between the sulfurs of half-cystine residues, and not a constituent of the molybdenum cofactor. The action of selenite was directed to the cytoplasmic species of carbon monoxide oxidase exclusively, whereas the CO----methylene blue activity of the membrane-bound enzyme remained unaffected.

Duke Scholars

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

May 10, 1984

Volume

259

Issue

9

Start / End Page

5612 / 5617

Location

United States

Related Subject Headings

  • Selenium
  • Selenious Acid
  • Pseudomonas
  • Protein Binding
  • Methylene Blue
  • Kinetics
  • Enzyme Activation
  • Biochemistry & Molecular Biology
  • Aldehyde Oxidoreductases
  • 34 Chemical sciences
 

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

May 10, 1984

Volume

259

Issue

9

Start / End Page

5612 / 5617

Location

United States

Related Subject Headings

  • Selenium
  • Selenious Acid
  • Pseudomonas
  • Protein Binding
  • Methylene Blue
  • Kinetics
  • Enzyme Activation
  • Biochemistry & Molecular Biology
  • Aldehyde Oxidoreductases
  • 34 Chemical sciences