Related Experiment Video
Updated: Jul 8, 2026

Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
Published on: May 23, 2025
The occurrence of a novel NADH dehydrogenase, distinct from the old yellow enzyme, in Gluconobacter strains
Emiko Shinagawa1, Yoshitaka Ano, Osao Adachi
1Department of Chemical and Biological Engineering, Ube National College of Technology, Tokiwadai, Ube, Japan. emiko@ube-k.ac.jp
Abstract:
A novel NADH dehydrogenase (NADH-dh) involving FAD as coenzyme, distinct from NADPH dehydrogenase (NADPH-dh, old yellow enzyme, EC 1.6.99.1), was found in the same cytoplasmic fraction of Gluconobacter strains. Conventional artificial electron acceptors were more effective than molecular oxygen in the NADH-dh reaction. NADH-dh did not appear to be identical with any previously described flavoproteins, although the N-terminal amino acid sequence showed 100% similarity with a non-heme chloroperoxidase. The N-terminal amino acid sequence of NADPH-dh matched 100% a putative oxidoreductase containing the old yellow enzyme-like FMN-binding domain. NADH-dh might function to regenerate NAD coupling with NAD-dependent dehydrogenases in the cytoplasm of Gluconobacter strains.
More Related Videos
08:57Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
Published on: February 24, 2018
06:45Monitoring Intraspecies Competition in a Bacterial Cell Population by Cocultivation of Fluorescently Labelled Strains
Published on: January 18, 2014
Related Concept Videos
Anoxygenic Photosynthesis
Anoxygenic Phototrophic Bacteria
Other Glycolytic Pathways
Role of Reduced Coenzymes NADH and FADH₂
Exon Recombination
Exon shuffling follows “splice frame rules.” Each exon has three reading...
Genome Size and the Evolution of New Genes