Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Membrane-bound flavin adenine dinucleotide in Methanobacterium bryantii

Journal Article · · Biochem. Biophys. Res. Commun.; (United States)

Noncovalently attached flavin was isolated and partially purified from the membrane fraction of Methanobacterium bryantii. The flavin was identified as FAD by absorption and fluorescence spectroscopy, effects on the spectra of reduction and of protonation, phenol extractability, behavior in thin layer chromatography in two solvent systems, and ability to reconstitute activity of the FAD-specific enzyme D-amino acid oxidase. These singular organisms thus are capable of synthesizing isoalloxizine-type flavins as well as the unique 5-deazaflavin factor F/sub 420/. Membrane-bound FAD may thus (in addition to iron-sulfur centers and a nickel species) be involved in energy-coupled methanogenesis.

Research Organization:
Utah State Univ., Logan
OSTI ID:
5209706
Journal Information:
Biochem. Biophys. Res. Commun.; (United States), Journal Name: Biochem. Biophys. Res. Commun.; (United States) Vol. 100:1; ISSN BBRCA
Country of Publication:
United States
Language:
English