Bacterial selenoenzymes and mechanisms of action
- 1 January 2001
- book chapter
- Published by Springer Nature
Abstract
No abstract availableKeywords
This publication has 34 references indexed in Scilit:
- MOLYBDENUM-COFACTOR–CONTAINING ENZYMES: Structure and MechanismAnnual Review of Biochemistry, 1997
- The Mononuclear Molybdenum EnzymesChemical Reviews, 1996
- Properties of the Selenium- and Molybdenum-Containing Nicotinic Acid Hydroxylase from Clostridium barkeriBiochemistry, 1996
- Nicotinic acid hydroxylase from Clostridium barkeri: electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme.Proceedings of the National Academy of Sciences, 1994
- Occurrence of molybdenum in the nicotinic acid hydroxylase from Clostridium barkeriArchives of Biochemistry and Biophysics, 1983
- Properties of the selenium-containing moiety of nicotinic acid hydroxylase from Clostridium barkeriArchives of Biochemistry and Biophysics, 1982
- Nicotinic acid hydroxylase fromClostridium barkeri:Selenium-dependent formation of active enzymeFEMS Microbiology Letters, 1979
- Chemical characterization of the selenoprotein component of clostridial glycine reductase: identification of selenocysteine as the organoselenium moiety.Proceedings of the National Academy of Sciences, 1976
- Purification of protein components of the clostridial glycine reductase system and characterization of protein A as a selenoproteinArchives of Biochemistry and Biophysics, 1973
- The need for selenite and molybdate in the formation of formic dehydrogenase by members of the Coli-aerogenes group of bacteriaBiochemical Journal, 1954