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Journal Article
FEBS Letters, ISSN 0014-5793, 2013, Volume 587, Issue 14, pp. 2214 - 2218
•Cytochrome bd from E. coli displays a notable catalase activity.•Thermal denaturation or complete reduction of cytochrome bd abolishes this activity.•Activity... 
Oxidative stress | Reactive oxygen species | Respiratory chain | Hemeprotein | Bacteria–host interaction | Microbial metabolism | N-ethylmaleimide | dithiothreitol | DTT | NEM | ROS | reactive oxygen species | 2,3-dimethoxy-5-methyl-6-(3-methyl-2-butenyl)-1,4-benzoquinone | Bacteria-host interaction | AEROBIC RESPIRATORY-CHAIN | OXYGEN-REDUCING SITE | BIOCHEMISTRY & MOLECULAR BIOLOGY | DI-HEME | HIGH-AFFINITY | TERMINAL OXIDASE | CELL BIOLOGY | BIOPHYSICS | QUINOL OXIDASE | CARBON-MONOXIDE | NITRIC-OXIDE | HYDROGEN-PEROXIDE | C-OXIDASE | Oxidoreductases - antagonists & inhibitors | Cytochromes - chemistry | Oxidative Stress | Hydroquinones - chemistry | Sodium Cyanide - chemistry | Oxidoreductases - chemistry | Hydrogen Peroxide - chemistry | NAD - chemistry | Cattle | Enzyme Inhibitors - chemistry | Oxygen - chemistry | Electron Transport Chain Complex Proteins - antagonists & inhibitors | Dithiothreitol - chemistry | Escherichia coli Proteins - antagonists & inhibitors | Reducing Agents - chemistry | NAD(P)H Dehydrogenase (Quinone) - chemistry | Cytochromes - antagonists & inhibitors | Escherichia coli - enzymology | Oxidants - chemistry | Rats | Electron Transport Chain Complex Proteins - chemistry | Animals | Kinetics | Escherichia coli Proteins - chemistry | Catalase - chemistry | Proteins | Oxidases | Denaturation | Nitric oxide | Escherichia coli | Oxygen | Enzyme Inhibitors | Hydrogen Peroxide | Biochemistry, Molecular Biology | Sodium Cyanide | Reducing Agents | NAD(P)H Dehydrogenase (Quinone) | NAD | Life Sciences | Hydroquinones | Escherichia coli Proteins | Catalase | Oxidants | Cytochromes | Oxidoreductases | Dithiothreitol | Electron Transport Chain Complex Proteins
Journal Article
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2017, Volume 292, Issue 34, pp. 14039 - 14049
Flavin-based electron transfer bifurcation is emerging as a fundamental and powerful mechanism for conservation and deployment of electrochemical energy in... 
electron bifurcation | FLAVODOXIN | PROTEIN | ACID | NITROREDUCTASE | transient absorption spectroscopy | BIOCHEMISTRY & MOLECULAR BIOLOGY | EXCITED-STATE DYNAMICS | flavin | DESULFOVIBRIO-VULGARIS | NADH OXIDASE | electron transfer | fluorescence | flavoprotein | PURIFICATION | PHOTOACTIVATION | BINDING | energetics | Flavin-Adenine Dinucleotide - chemistry | Nitroreductases - genetics | Electron Transport | ortho-Aminobenzoates - chemistry | Flavodoxin - genetics | Nitroreductases - chemistry | Enterobacter cloacae - enzymology | Bacterial Proteins - chemistry | Flavodoxin - chemistry | Multienzyme Complexes - metabolism | Holoenzymes - chemistry | Oxidoreductases - chemistry | Recombinant Fusion Proteins - metabolism | Flavin-Adenine Dinucleotide - metabolism | Silent Mutation | Holoenzymes - metabolism | Apoenzymes - metabolism | NADH, NADPH Oxidoreductases - chemistry | NADH, NADPH Oxidoreductases - metabolism | Pyrococcus furiosus - enzymology | Recombinant Proteins - metabolism | NADH, NADPH Oxidoreductases - genetics | Thermus thermophilus - enzymology | Flavodoxin - metabolism | Biocatalysis | Oxidation-Reduction | Oxidoreductases - metabolism | Oxidoreductases - genetics | Benzoic Acid - metabolism | Bacterial Proteins - genetics | Models, Molecular | Recombinant Proteins - chemistry | Flavin-Adenine Dinucleotide - analogs & derivatives | Multienzyme Complexes - genetics | Recombinant Fusion Proteins - chemistry | Multienzyme Complexes - chemistry | Nitroreductases - metabolism | Apoenzymes - genetics | Apoenzymes - chemistry | Benzoic Acid - chemistry | Bacterial Proteins - metabolism | Desulfovibrio vulgaris - enzymology | Holoenzymes - genetics | ortho-Aminobenzoates - metabolism | solar (fuels), biofuels (including algae and biomass), bio-inspired, hydrogen and fuel cells | Bioenergetics
Journal Article
PLOS ONE, ISSN 1932-6203, 03/2014, Volume 9, Issue 3, p. e91809
Condensed tannins from Ficus virens leaves, fruit, and stem bark were isolated and their structures characterized by C-13 nuclear magnetic resonance... 
SKIN PIGMENTATION | IN-VITRO | TOF MS ANALYSIS | MUSHROOM TYROSINASE | KINETICS | MULTIDISCIPLINARY SCIENCES | LEAVES | DOPAMINE | IONS | HPLC | RADICAL SCAVENGING ACTIVITY | Oxidoreductases - antagonists & inhibitors | Plant Extracts - chemistry | Plant Extracts - pharmacology | Molecular Conformation | Chelating Agents - chemistry | Models, Molecular | Substrate Specificity | Monophenol Monooxygenase - antagonists & inhibitors | Chelating Agents - pharmacology | Proanthocyanidins - chemistry | Copper - chemistry | Proanthocyanidins - pharmacology | Nuclear Magnetic Resonance, Biomolecular | Molecular Structure | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Catalysis | Ficus - chemistry | Monophenol Monooxygenase - chemistry | Polymerization | Biological products | Ionization | Mass spectrometry | Quinone | High performance liquid chromatography | Tannic acid | Procyanidins | Nuclear magnetic resonance--NMR | Enzyme activity | Molecular structure | Ecosystems | Bark | Fluorescence | Molecular docking | Fruits | Wetlands | Leaves | Quinones | Tannins | Enzymatic activity | Lasers | Education | Life sciences | Inhibition | Copper | Hydroxyl groups | Food | Spectroscopy | Enzymes | Free radicals | Magnetic resonance | Ions | Mass spectroscopy | Desorption | Liquid chromatography | High-performance liquid chromatography | Chromatography | Quenching | Flavonoids | Phytochemicals | Molecular modelling | Inhibitors | Scientific imaging | Chelates | Tyrosinase | Nuclear magnetic resonance | NMR
Journal Article