Reference

Anaerobic oxidation of 1,5-pentanediol, 2-butanol, and 2-propanol by a newly isolated sulfate-reducer

Anaerobic oxidation of 1,5-pentanediol, 2-butanol, and 2-propanol by a newly isolated sulfate-reducer. Tanaka, Kazuhiro (Ferment. Res. Inst., Tsukuba 305, Japan). J. Ferment. Bioeng., 73(5), 362-5 (English) 1992. CODEN: JFBIEX. ISSN: 0922-338X. DOCUMENT TYPE: Journal CA Section: 10 (Microbial, Algal, and Fungal Biochemistry) A strain (strain IsBd1) of anaerobic bacterium was isolated in pure culture from a sand sample of Lake Kasumigaura using 1,4-butanediol as a sole electron-donor source, and was characterized. The bacterium was motile with a single polar flagellum and stained Gram-neg. Spores were never obsd. Sulfate, sulfite, thiosulfate, and elemental sulfur were reduced with concomitant growth. Even in the presence of excess sulfate, 1,4-butanediol and 1,5-pentanediol were oxidized stoichiometrically to 4-hydroxybutyrate and 5-hydroxyvalerate, resp.; 2-propanol and 2-butanol were oxidized stoichiometrically to corresponding ketones. Interspecies hydrogen transfer occurred between the isolate and Methanospirillum hungatei with ethanol, 1,3-butanediol, 1,4-butanediol, 1-butanol, 2-butanol, 2-methoxyethanol, 1,5-pentanediol, 1,3-propanediol, 1-propanol, and 2-propanol. Chemolithoheterotrophic growth was possible with formate or hydrogen and acetate in the presence of sulfate. Acetoin was fermented to acetate, 2,3-butanediol, and ethanol. Fumarate and L-malate were fermented to acetate and succinate. S-1,2-Propanediol was fermented to 1-propanol and propionate, but a racemic mixt. was not fermented. When formate or hydrogen was supplied, fumarate and L-malate were reduced stoichiometrically to succinate with growth. The DNA base ratio of the isolate was 53 mol% guanine plus cytosine. Strain IsBd1 was identified as a member of the genus Desulfovibrio.

Inactivation of propanediol oxidoreductase of Escherichia coli by metal-catalyzed oxidation

Inactivation of propanediol oxidoreductase of Escherichia coli by metal-catalyzed oxidation. Cabiscol, Elisa; Badia, Josefa; Baldoma, Laura; Hidalgo, Elena; Aguilar, Juan; Ros, Joaquim (Sch. Med., Univ. Barcelona, Lleida 08028, Spain). Biochim. Biophys. Acta, 1118(2), 155-60 (English) 1992. CODEN: BBACAQ. ISSN: 0006-3002. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) 1,2-Propanediol oxidoreductase (lactaldehyde reductase) (I), which reduces the L-lactaldehyde formed in the fermn. of L-fucose or L-rhamnose to L-1,2-propanediol in E. coli, was inactivated by a component of E. coli cell exts. in the presence of O2. I prepns. were shown to be inactivated in vitro by aerobic incubations in the presence of Fe3+ and ascorbate. The Fe3+ ascorbate-mediated inactivation reaction was inhibited by catalase, although not by superoxide dismutase. Under anaerobic conditions, the presence of H2O2 strongly inactivated the enzyme. I was rapidly degraded in the presence of O2, whereas the native enzyme displayed high stability as long as no O2 was present.