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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
Zeitschrift für Naturforschung C, ISSN 0939-5075, 02/2019, Volume 74, Issue 3, pp. 101 - 104
There is an increasing interest in the application of peroxygenases in biocatalysis, because of their ability to catalyse the oxyfunctionalisation reaction in... 
old yellow enzyme | formate dehydrogenase | hydrogen peroxide generation | oxyfunctionalisation | peroxygenase | Hydrogen peroxide generation | Formate dehydrogenase | Oxyfunctionalisation | Old yellow enzyme | Peroxygenase | OXIDATION | SYSTEM | YELLOW ENZYME HOMOLOG | EVOLUTION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ELECTRODE | PHARMACOLOGY & PHARMACY | Fungal Proteins - chemistry | Carbon Dioxide - chemistry | Formates - chemistry | Stereoisomerism | Bacterial Proteins - chemistry | Mixed Function Oxygenases - metabolism | Candida - enzymology | Mixed Function Oxygenases - chemistry | Bacillus subtilis - chemistry | Oxygen - metabolism | Agrocybe - enzymology | NAD - chemistry | Coenzymes - metabolism | FMN Reductase - metabolism | Hydrogen Peroxide - chemical synthesis | Oxygen - chemistry | Agrocybe - chemistry | Coenzymes - chemistry | NAD - metabolism | Formates - metabolism | Biocatalysis | Carbon Dioxide - metabolism | Benzene Derivatives - metabolism | Hydroxylation | Oxidation-Reduction | Formate Dehydrogenases - metabolism | Bacillus subtilis - enzymology | Flavin Mononucleotide - chemistry | Hydrogen Peroxide - metabolism | Formate Dehydrogenases - chemistry | Candida - chemistry | FMN Reductase - chemistry | Bacterial Proteins - metabolism | Kinetics | Benzene Derivatives - chemistry | Flavin Mononucleotide - metabolism | Fungal Proteins - metabolism
Journal Article
Journal Article
PloS one, ISSN 1932-6203, 2017, Volume 12, Issue 8, p. e0182658
Moringa oleifera Lam. is a tropical plant, used for centuries as food and traditional medicine. The aim of this study was to develop, validate and... 
ANTITUMOR PROMOTER | ACTIVATION | NRF2 | CURCUMIN | NITRIC-OXIDE SYNTHASE | ANTIOXIDANT | MULTIDISCIPLINARY SCIENCES | NF-KB | GENE-EXPRESSION PROFILES | STRUCTURAL INFLUENCE | L | Plant Extracts - chemistry | Antioxidants - chemistry | Plant Extracts - pharmacology | Curcumin - chemistry | Anti-Inflammatory Agents, Non-Steroidal - chemistry | Male | Anti-Inflammatory Agents, Non-Steroidal - pharmacology | Moringa oleifera - chemistry | Inflammation - drug therapy | Isothiocyanates - chemistry | Hindlimb - immunology | Seeds - chemistry | Phytotherapy | Drug Evaluation, Preclinical | Disease Models, Animal | Phytochemicals - chemistry | Cell Line | Edema - immunology | Plant Extracts - isolation & purification | Edema - drug therapy | Inflammation - immunology | Antioxidants - pharmacology | Random Allocation | Rats, Sprague-Dawley | Phytochemicals - isolation & purification | Macrophages - metabolism | Animals | Antioxidants - isolation & purification | Hindlimb - drug effects | Macrophages - drug effects | Carrageenan | Phytochemicals - pharmacology | Curcuma - chemistry | Antioxidants | Anti-inflammatory drugs | Physiological aspects | Research | Properties | Materia medica, Vegetable | Plant extracts | Disorders | Plant biology | Lipopolysaccharides | Proteins | Interleukins | Glutathione transferase | Biocompatibility | Medicinal plants | Carbohydrates | Enzymes | Cytokines | Gene expression | Fatty acids | Anti-inflammatory agents | Studies | Mitigation | Flavonoids | Nitric oxide | Minimum inhibitory concentration | Fats | In vitro methods and tests | Enrichment | Oxidative stress | Food plants | Seeds | Oxidoreductase | Kinases | Inflammatory diseases | Optimization | Interleukin 6 | Rodents | Heme | Interleukin 1 | Glycosides | Tumor necrosis factor-TNF | Curcumin | Nonsteroidal anti-inflammatory drugs | Pharmaceutical sciences | Glutathione | Food | Chronic illnesses | Edema | Aspirin | Isothiocyanate | Inflammation | NAD | Natural products | Phenols | Cancer
Journal Article
Journal Article
Journal Article
Scientific reports, ISSN 2045-2322, 02/2016, Volume 6, Issue 1, p. 20629
Glyoxylate accumulation within cells is highly toxic. In humans, it is associated with hyperoxaluria type 2 (PH2) leading to renal failure. The glyoxylate... 
HYDROXYPYRUVATE REDUCTASE | PROTEIN | GENE | SPECIFICITY | STRUCTURAL BASIS | MULTIDISCIPLINARY SCIENCES | SEQUENCE | MODEL | EXPRESSION | DEHYDROGENASE | ARCHAEAL GLYOXYLATE REDUCTASE | Hydroxypyruvate Reductase - chemistry | Pyrococcus furiosus - chemistry | Hydroxypyruvate Reductase - genetics | Glyoxylates - chemistry | Archaeal Proteins - chemistry | Substrate Specificity | Crystallography, X-Ray | Pyrococcus - enzymology | NADP - chemistry | Alcohol Oxidoreductases - genetics | NAD - chemistry | Pyrococcus - chemistry | Escherichia coli - metabolism | Archaeal Proteins - genetics | NADP - metabolism | Protein Stability | Hydroxypyruvate Reductase - metabolism | NAD - metabolism | Pyrococcus furiosus - enzymology | Archaeal Proteins - metabolism | Pyruvates - metabolism | Recombinant Proteins - metabolism | Catalytic Domain | Gene Expression | Pyrococcus horikoshii - chemistry | Models, Molecular | Recombinant Proteins - chemistry | Alcohol Oxidoreductases - metabolism | Glyceric Acids - chemistry | Enzyme Assays | Recombinant Proteins - genetics | Pyrococcus horikoshii - enzymology | Glyceric Acids - metabolism | Glyoxylates - metabolism | Alcohol Oxidoreductases - chemistry | Escherichia coli - genetics | Pyruvates - chemistry | Protein Binding | Kinetics | Enzymes | NADH | Kidneys | Renal failure | Hyperoxaluria | NADP | Kidney transplantation | Life Sciences | Biomolecules | Biochemistry, Molecular Biology
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2015, Volume 290, Issue 34, pp. 20761 - 20773
Complex I (NADH:ubiquinone oxidoreductase) is a multisubunit, membrane-bound enzyme of the respiratory chain. The energy from NADH oxidation in the peripheral... 
3-DIMENSIONAL STRUCTURE | CONSERVED CHARGED RESIDUES | SUBUNIT NUOL | ESCHERICHIA-COLI NDH-1 | ATP SYNTHASE | UBIQUINONE OXIDOREDUCTASE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ELECTRON-MICROSCOPY | MEMBRANE DOMAIN | NADH-QUINONE OXIDOREDUCTASE | Protons | Periplasm - enzymology | Molecular Sequence Data | NADH Dehydrogenase - genetics | Structure-Activity Relationship | Electron Transport Complex I - metabolism | NAD - chemistry | Copper - chemistry | Electron Transport Complex I - genetics | Cysteine - metabolism | Periplasm - chemistry | NAD - metabolism | Cytoplasm - chemistry | Protein Structure, Tertiary | Amino Acid Sequence | Cytoplasm - enzymology | Gene Expression | Cross-Linking Reagents - chemistry | Escherichia coli - enzymology | Protein Structure, Secondary | Models, Molecular | Escherichia coli Proteins - metabolism | Cysteine - chemistry | Escherichia coli - chemistry | NADH Dehydrogenase - chemistry | NADH Dehydrogenase - metabolism | Plasmids - metabolism | Electron Transport Complex I - chemistry | Escherichia coli - genetics | Plasmids - chemistry | Escherichia coli Proteins - genetics | Mutation | Escherichia coli Proteins - chemistry | methanethiosulfonate | proton transport | Bioenergetics | membrane energetics | complex I | membrane protein | cysteine-mediated cross-linking | protein cross-linking
Journal Article