Membrane-bound flavin adenine dinucleotide in Methanobacterium bryantii
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
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59 BASIC BIOLOGICAL SCIENCES
ABSORPTION SPECTROSCOPY
BACTERIA
CHROMATOGRAPHY
ELECTRON TRANSFER
EMISSION SPECTROSCOPY
ENZYME ACTIVITY
ENZYMES
FLUORESCENCE SPECTROSCOPY
HETEROCYCLIC COMPOUNDS
ISOALLOXAZINES
MEMBRANES
METHANOGENIC BACTERIA
MICROORGANISMS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
ORGANIC OXYGEN COMPOUNDS
OXIDOREDUCTASES
SEPARATION PROCESSES
SPECTRA
SPECTROSCOPY
THIN-LAYER CHROMATOGRAPHY