chiniofon and nicotinamide-hypoxanthine-dinucleotide

chiniofon has been researched along with nicotinamide-hypoxanthine-dinucleotide* in 1 studies

Other Studies

1 other study(ies) available for chiniofon and nicotinamide-hypoxanthine-dinucleotide

Article	Year
Enzymatic and energetic properties of the aerobic respiratory chain-linked NADH oxidase system in the marine bacterium Pseudomonas nautica. Molecules and cells, 2000, Aug-31, Volume: 10, Issue:4 Membranes of Pseudomonas nautica, grown aerobically on a complex medium, oxidized both NADH and deamino-NADH as substrates. The activity of membrane-bound NADH oxidase was activated by monovalent cations including Na+, Li+, and K+. The activation by Na+ was higher than that by Li+ and K+. The maximum activity of NADH oxidase was obtained at about pH 9.0 in the presence of 0.08 M NaCl. The NADH oxidase activity was completely inhibited by 60 microM 2-heptyl-4-hydroxyquinoline-N-oxide (HQNO), while the NADH:quinone oxidoreductase activity was about 37% inhibited by 60 microM HQNO. The activities of NADH oxidase and NADH:quinone oxidoreductase were about 40% inhibited by 60 microM rotenone. The fluorescence quenching technique revealed that electron transfer from NADH to ubiquinone-1 (Q-1) or oxygen generated a membrane potential (deltapsi) which was larger and more stable in the presence of Na+ than in the absence of Na+. However, the All was highly sensitive to a protonophore, carbonyl-cyanide m-chlorophenylhydrazone (CCCP) even at alkaline pH. Topics: Bacterial Proteins; Electron Transport; Hydrogen-Ion Concentration; Hydroxyquinolines; Membrane Potentials; Membrane Proteins; Multienzyme Complexes; NAD; NADH, NADPH Oxidoreductases; Oxygen; Potassium Cyanide; Pseudomonas; Quinone Reductases; Rotenone; Salts; Ubiquinone; Uncoupling Agents	2000

Article

Year

Enzymatic and energetic properties of the aerobic respiratory chain-linked NADH oxidase system in the marine bacterium Pseudomonas nautica.

Molecules and cells, 2000, Aug-31, Volume: 10, Issue:4

Membranes of Pseudomonas nautica, grown aerobically on a complex medium, oxidized both NADH and deamino-NADH as substrates. The activity of membrane-bound NADH oxidase was activated by monovalent cations including Na+, Li+, and K+. The activation by Na+ was higher than that by Li+ and K+. The maximum activity of NADH oxidase was obtained at about pH 9.0 in the presence of 0.08 M NaCl. The NADH oxidase activity was completely inhibited by 60 microM 2-heptyl-4-hydroxyquinoline-N-oxide (HQNO), while the NADH:quinone oxidoreductase activity was about 37% inhibited by 60 microM HQNO. The activities of NADH oxidase and NADH:quinone oxidoreductase were about 40% inhibited by 60 microM rotenone. The fluorescence quenching technique revealed that electron transfer from NADH to ubiquinone-1 (Q-1) or oxygen generated a membrane potential (deltapsi) which was larger and more stable in the presence of Na+ than in the absence of Na+. However, the All was highly sensitive to a protonophore, carbonyl-cyanide m-chlorophenylhydrazone (CCCP) even at alkaline pH.

Topics: Bacterial Proteins; Electron Transport; Hydrogen-Ion Concentration; Hydroxyquinolines; Membrane Potentials; Membrane Proteins; Multienzyme Complexes; NAD; NADH, NADPH Oxidoreductases; Oxygen; Potassium Cyanide; Pseudomonas; Quinone Reductases; Rotenone; Salts; Ubiquinone; Uncoupling Agents

2000