title: Two proteins with diaphorase activity from Clostridium thermocellum and Moorella thermoacetica.
abstract: Two high-molecular-weight rubredoxin genes (hrb) from Clostridium thermocellum and Moorella thermoacetica were expressed in Escherichia coli and their translated products (Hrb) were characterized. M. thermoacetica Hrb showed strong diaphorase activity. In contrast, C. thermocellum Hrb, containing neither FMN nor FAD in the molecule, showed flavin reductase activity with moderate diaphorase activity. Both enzymes were optimally active at about 50 degrees C.
authors.affiliation: Graduate School of Bioresources, Mie University, Tsu 514-8507, Japan.
authors.forename: Saikat
authors.initials: S
authors.lastname: Chakraborty
authors.forename: Makiko
authors.initials: M
authors.lastname: Sakka
authors.forename: Tetsuya
authors.initials: T
authors.lastname: Kimura
authors.forename: Kazuo
authors.initials: K
authors.lastname: Sakka
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics* / Q000502:physiology*; D048013:Acetivibrio thermocellus / Q000201:enzymology*; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D009245:NADH Dehydrogenase; D010088:Oxidoreductases; D012416:Rubredoxins
chemical_list: D001426:Bacterial Proteins; D012416:Rubredoxins; D010088:Oxidoreductases; D009245:NADH Dehydrogenase