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1. A Structural Perspective on Respiratory Complex I
: Structure and Function of NADH:ubiquinone oxidoreductase
by Sazanov, Leonid
2012, ISBN 9789400741386
Oxidoreductases
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2. Full Text Sub-State Conformations of the Mesophilic and Psychrophilic Lactate Dehydrogenases Preceding Irreversible Thermal Inactivation
by Khrapunov, Sergei and Chang, Eric and Callender, Robert
Biophysical Journal, ISSN 0006-3495, 02/2017, Volume 112, Issue 3, pp. 56a - 57a
Oxidoreductases
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3. Full Text Discovery of BI 135585, an in vivo efficacious oxazinanone-based 11[beta] hydroxysteroid dehydrogenase type 1 inhibitor
by Zhuang, Linghang and Tice, Colin M and Xu, Zhenrong and Zhao, Wei and Cacatian, Salvacion and Ye, Yuan-Jie and Singh, Suresh B and Lindblom, Peter and McKeever, Brian M and Krosky, Paula M and Zhao, Yi and Lala, Deepak and Kruk, Barbara A and Meng, Shi and Howard, Lamont and Johnson, Judith A and Bukhtiyarov, Yuri and Panemangalore, Reshma and Guo, Joan and Guo, Rong and Himmelsbach, Frank and Hamilton, Bradford and Schuler-Metz, Annette and Schauerte, Heike and Gregg, Richard and McGeehan, Gerard M and Leftheris, Katerina and Claremon, David A
Bioorganic & Medicinal Chemistry, ISSN 0968-0896, 07/2017, Volume 25, Issue 14, p. 3649
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4. Full Text Carbon fixation via the formate dehydrogenases of Shewanella
by Davies, Jonathan and Clarke, Tom and Butt, Julea and Richardson, David
New BIOTECHNOLOGY, ISSN 1871-6784, 07/2016, Volume 33, pp. S110 - S110
Oxidoreductases
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5. Structure and functions of amine oxidases
by Mondovì, Bruno
1985, ISBN 9780849358692, 285
Amine oxidase
Book
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6. Full Text Evolution of cytochrome bc complexes: From membrane-anchored dehydrogenases of ancient bacteria to triggers of apoptosis in vertebrates
by Dibrova, Daria V and Cherepanov, Dmitry A and Galperin, Michael Y and Skulachev, Vladimir P and Mulkidjanian, Armen Y
BBA - Bioenergetics, ISSN 0005-2728, 11/2013, Volume 1827, Issue 11-12, pp. 1407 - 1427
This review traces the evolution of the cytochrome complexes from their early spread among prokaryotic lineages and up to the mitochondrial cytochrome complex... 
ubiquinone | Bioenergetics, molecular evolution, ubiquinol:cytochrome c oxidoreductase | cytochrome c | plastoquinone | cardiolipin, cell death, photosynthesis, apoptosome | Bioenergetics, molecular evolution, ubiquinol | cardiolipin, cell death, photosynthesis | apoptosome | cytochrome c oxidoreductase | IRON-SULFUR PROTEIN | INNER MITOCHONDRIAL-MEMBRANE | PURPLE PHOTOSYNTHETIC BACTERIA | BIOCHEMISTRY & MOLECULAR BIOLOGY | OXYGEN SPECIES GENERATION | X-RAY-STRUCTURE | ACTIVATED Q-CYCLE | TARGETED PLASTOQUINONE DERIVATIVES | TRANSMEMBRANE PROTON-TRANSFER | BIOPHYSICS | ANAEROBIC AMMONIUM OXIDATION | Bioenergetics, molecular evolution, ubiquinol: cytochrome c oxidoreductase | UNIVERSAL COMMON ANCESTOR | Electron Transport Complex III - chemistry | Cytochrome b6f Complex - metabolism | Electron Transport Complex III - genetics | Electron Transport Complex III - metabolism | Oxidoreductases - metabolism | Vertebrates - genetics | Membrane Proteins - genetics | Oxidoreductases - genetics | Humans | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Models, Molecular | Apoptosis - genetics | Oxidoreductases - chemistry | Cytochrome b6f Complex - genetics | Animals | Membrane Proteins - chemistry | Cytochrome b6f Complex - chemistry | Bacterial Proteins - metabolism | Protein Conformation | Membrane Proteins - metabolism | Evolution, Molecular | Membrane lipids | Cytochrome b | Analysis | Bacteria | Mitochondrial DNA | Cardiolipin | Oxidoreductases | Apoptosis
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7. Full Text Metabolic reprogramming of Vibrio cholerae impaired in respiratory NADH oxidation is accompanied by increased copper sensitivity
by Toulouse, Charlotte and Metesch, Kristina and Pfannstiel, Jens and Steuber, Julia
Journal of Bacteriology, ISSN 0021-9193, 08/2018, Volume 200, Issue 15
The electrogenic, sodium ion-translocating NADH: quinone oxidoreductase (NQR) from Vibrio cholerae is frequent in pathogenic bacteria and a potential target... 
Nontraditional drug target | Vibrio cholerae | translocating NADH:quinone oxidoreductase | Sodium-translocating NADH:quinone oxidoreductase | Comparative proteomics | Copper tolerance | Sodium bioenergetics | NQR | comparative proteomics | PROTEIN | UBIQUINONE OXIDOREDUCTASE | ESCHERICHIA-COLI | MICROBIOLOGY | IDENTIFICATION | VIRULENCE | copper tolerance | TRANSPORT | SUBSTRATE-BINDING | Na+-translocating NADH: quinone oxidoreductase | QUINONE OXIDOREDUCTASE | sodium-translocating NADH: quinone oxidoreductase | GROWTH | GENE-EXPRESSION | sodium bioenergetics | nontraditional drug target | Copper Sulfate - pharmacology | Energy Metabolism | Oxidation-Reduction | Vibrio cholerae - pathogenicity | Virulence | Bacterial Proteins - genetics | Bacterial Proteins - metabolism | Gene Expression Regulation, Bacterial - physiology | NAD - metabolism | Vibrio cholerae - drug effects | Vibrio cholerae - metabolism
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8. Quinones and Quinone enzymes. Part B
by Sies, Helmut and Packer, Lester
2004, Methods in Enzymology, ISBN 0121827860, Volume 382, xxxviii, 572
Quinones are members of a class of aromatic compounds with two oxygen atoms bonded to the ring as carbonyl groups. This volume covers more clinical aspects of... 
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9. Full Text Na+-NQR (Na+-translocating NADH:ubiquinone oxidoreductase) as a novel target for antibiotics
by Dibrov, Pavel and Dibrov, Elena and Pierce, Grant N
FEMS Microbiology Reviews, ISSN 0168-6445, 09/2017, Volume 41, Issue 5, pp. 653 - 671
Abstract The recent breakthrough in structural studies on Na+-translocating NADH:ubiquinone oxidoreductase (Na+-NQR) from the human pathogen Vibrio cholerae... 
Na+-translocating NADH:ubiquinone oxidoreductase | Na+ circulation | Na+-NQR | antibiotic design | genome analysis | sodium-motive force | CHLAMYDIA-PNEUMONIAE | Na+-translocating NADH: ubiquinone oxidoreductase | ESCHERICHIA-COLI | PUMPING NADHQUINONE OXIDOREDUCTASE | MICROBIOLOGY | ENERGY-CONSERVATION | MULTIDRUG EFFLUX PUMP | GRAM-NEGATIVE BACTERIA | QUINONE OXIDOREDUCTASE | COMPLEX-I | MARINE VIBRIO-ALGINOLYTICUS | 2-N-HEPTYL-4-HYDROXYQUINOLINE N-OXIDE | Vibrio cholerae - enzymology | Electron Transport Complex I - antagonists & inhibitors | Enzyme Inhibitors - metabolism | Anti-Bacterial Agents - metabolism | Drug Discovery | Electron Transport Complex I - metabolism | Drug Delivery Systems | Water-borne diseases | NADH-ubiquinone oxidoreductase | Pathogens | Enzymes | Energy metabolism | Oxidoreductase | Virulence | Antimicrobial agents | Pharmacology | Na+/K+-exchanging ATPase | Metabolism | Drug development | Molecular chains | Ubiquinone | Inhibitors | NADH | Sodium | Antibiotics | Nicotinamide adenine dinucleotide | Ubiquinone oxidoreductase | Vibrio
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10. Full Text Selective BRAFV600E inhibition enhances T-cell recognition of melanoma without affecting lymphocyte function
by Boni, Andrea and Cogdill, Alexandria P and Dang, Ping and Udayakumar, Durga and Njauw, Ching-Ni Jenny and Sloss, Callum M and Ferrone, Cristina R and Flaherty, Keith T and Lawrence, Donald P and Fisher, David E and Tsao, Hensin and Wargo, Jennifer A
Cancer Research, ISSN 0008-5472, 07/2010, Volume 70, Issue 13, pp. 5213 - 5219
Targeted therapy against the BRAF/mitogen-activated protein kinase (MAPK) pathway is a promising new therapeutic approach for the treatment of melanoma.... 
Intramolecular Oxidoreductases - biosynthesis | Intramolecular Oxidoreductases - immunology | Diphenylamine - pharmacology | Nitriles - pharmacology | Humans | Membrane Glycoproteins - biosynthesis | Antigens, Neoplasm - biosynthesis | Neoplasm Proteins - immunology | Extracellular Signal-Regulated MAP Kinases - antagonists & inhibitors | Melanoma - enzymology | Extracellular Signal-Regulated MAP Kinases - metabolism | gp100 Melanoma Antigen | Diphenylamine - analogs & derivatives | T-Lymphocytes - drug effects | Benzamides - pharmacology | Epitopes, T-Lymphocyte - immunology | Membrane Glycoproteins - immunology | Neoplasm Proteins - genetics | Proto-Oncogene Proteins B-raf - metabolism | Oxidoreductases - biosynthesis | Antigens, Neoplasm - genetics | Butadienes - pharmacology | Antigens, Neoplasm - immunology | Neoplasm Proteins - biosynthesis | Oxidoreductases - genetics | Combined Modality Therapy | Membrane Glycoproteins - genetics | Proto-Oncogene Proteins B-raf - antagonists & inhibitors | Oxidoreductases - immunology | MAP Kinase Signaling System - drug effects | Intramolecular Oxidoreductases - genetics | Melanoma - immunology | Melanoma - drug therapy | Cell Line, Tumor | MART-1 Antigen | T-Lymphocytes - immunology | Melanoma - therapy
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11. Full Text Rare merosesquiterpenoids from basidiomycete Craterellus odoratus and their inhibition of 11[beta]-hydroxysteroid dehydrogenases
by Zhang, Ling and Shen, Yu and Wang, Fei and Leng, Ying and Liu, Ji-Kai
Phytochemistry, ISSN 0031-9422, 01/2010, Volume 71, Issue 1
Merosesquiterpenids, craterellins A-C (1-3), were isolated from cultures of the basidiomycete Craterellus odoratus together with the previously known... 
Oxidoreductases
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12. Full Text Mechanism and impact of catecholamine conversion by Vibrio cholerae
by Toulouse, Charlotte and Schmucker, Sonja and Metesch, Kristina and Pfannstiel, Jens and Michel, Bernd and Starke, Ines and Möller, Heiko M and Stefanski, Volker and Steuber, Julia
BBA - Bioenergetics, ISSN 0005-2728, 06/2019, Volume 1860, Issue 6, pp. 478 - 487
Bacterial pathogens are influenced by signaling molecules including the catecholamines adrenaline and noradrenaline which are host-derived hormones and... 
Adrenochrome | Superoxide | Na+ − NADH:quinone oxidoreductase | Vibrio cholerae | Adrenaline | NQR | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | INVOLVEMENT | IRON | NADH-QUINONE OXIDOREDUCTASE | TRANSLOCATING NADHQUINONE OXIDOREDUCTASE | Na+ - NADH:quinone oxidoreductase | NADHUBIQUINONE OXIDOREDUCTASE | BIOPHYSICS | TRANSFERRIN | ENTEROBACTIN | EPINEPHRINE
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13. Springer handbook of enzymes
: EC 1 / Supplement Volume S8, Class 1, Oxidoreductases
by Schomburg, D. (Dietmar) and Schomburg, Ida, 1954 and Chang, Antje and ebrary, Inc
2013, 2nd ed., Springer handbook of enzymes, ISBN 3642362648, Volume v. Suppl. 8
Enzymes | Oxidoreductases
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14. Full Text Structural, Biochemical, and Evolutionary Characterizations of Glyoxylate/Hydroxypyruvate Reductases Show Their Division into Two Distinct Subfamilies
by Kutner, Jan and Shabalin, Ivan G and Matelska, Dorota and Handing, Katarzyna B and Gasiorowska, Olga and Sroka, Piotr and Gorna, Maria W and Ginalski, Krzysztof and Wozniak, Krzysztof and Minor, Wladek and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Biochemistry, ISSN 0006-2960, 02/2018, Volume 57, Issue 6, pp. 963 - 977
The d-2-hydroxyacid dehydrogenase (2HADH) family illustrates a complex evolutionary history with multiple lateral gene transfers and gene duplications and... 
HYDROXYPYRUVATE REDUCTASE | FORMATE DEHYDROGENASE | SUBSTRATE-SPECIFICITY | PROTEIN | COLEUS-BLUMEI | BIOCHEMISTRY & MOLECULAR BIOLOGY | GLYOXYLATE REDUCTASE | ESCHERICHIA-COLI | PURIFICATION | D-LACTATE DEHYDROGENASE | MODEL | Hydroxypyruvate Reductase - chemistry | Sinorhizobium meliloti - genetics | Hydroxypyruvate Reductase - classification | Hydroxypyruvate Reductase - genetics | Sinorhizobium meliloti - enzymology | Bacterial Proteins - chemistry | Substrate Specificity | Crystallography, X-Ray | Alcohol Oxidoreductases - classification | Phylogeny | Alcohol Oxidoreductases - genetics | Sinorhizobium meliloti - chemistry | Aldehyde Oxidoreductases - chemistry | Hydroxypyruvate Reductase - metabolism | Aldehyde Oxidoreductases - classification | Bacterial Proteins - genetics | Models, Molecular | Alcohol Oxidoreductases - metabolism | Aldehyde Oxidoreductases - genetics | Sinorhizobium meliloti - metabolism | Aldehyde Oxidoreductases - metabolism | Alcohol Oxidoreductases - chemistry | Bacterial Proteins - metabolism | Protein Conformation | Bacterial Proteins - classification | Kinetics | Pyruvates | Genetic transformation | Chemical properties | Structure | Analysis
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15. Full Text Mitochondrial complex i
by Hirst, Judy
Annual Review of Biochemistry, ISSN 0066-4154, 06/2013, Volume 82, Issue 1, pp. 551 - 575
Complex I (NADH: ubiquinone oxidoreductase) is crucial for respiration in many aerobic organisms. In mitochondria, it oxidizes NADH from the tricarboxylic acid... 
Electron transport chain | Complex I dysfunction | Electron transfer | NADH:ubiquinone oxidoreductase | Superoxide production | Proton transfer | superoxide production | CONSERVED CHARGED RESIDUES | OXIDATIVE-PHOSPHORYLATION | electron transport chain | SUPEROXIDE-PRODUCTION | BOVINE HEART-MITOCHONDRIA | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | complex I dysfunction | proton transfer | MEMBRANE DOMAIN | IRON-SULFUR CLUSTERS | electron transfer | QUINONE OXIDOREDUCTASE | PROTON TRANSLOCATION | NADH-UBIQUINONE OXIDOREDUCTASE | Electron Transport | Electron Transport Complex I - chemistry | Reactive Oxygen Species - metabolism | Oxidation-Reduction | Humans | Ubiquinone - metabolism | Mitochondria - metabolism | Electron Transport Complex I - metabolism | Flavins - metabolism | Physiological aspects | Reactive oxygen species | Mitochondria | Oxidoreductases
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16. Full Text The mechanism of coupling between oxido‐reduction and proton translocation in respiratory chain enzymes
by Papa, Sergio and Capitanio, Giuseppe and Papa, Francesco
Biological Reviews, ISSN 1464-7931, 02/2018, Volume 93, Issue 1, pp. 322 - 349
ABSTRACT The respiratory chain of mitochondria and bacteria is made up of a set of membrane‐associated enzyme complexes which catalyse sequential, stepwise... 
ubiquinone cytochrome c oxidoreductase | cytochrome c oxidase | NADH‐ubiquinone oxidoreductase | redox proton pump | mitochondria | respiratory chain | NADH-ubiquinone oxidoreductase | BC COMPLEX | OXIDATIVE-PHOSPHORYLATION | CRYSTAL-STRUCTURE | MITOCHONDRIAL ELECTRON-TRANSPORT | NADH-QUINONE OXIDOREDUCTASE | IRON-SULFUR CLUSTERS | CYTOCHROME-C-OXIDASE | BIOLOGY | BOVINE COMPLEX-I | ENERGY TRANSDUCTION | POLYPEPTIDE SUBUNITS | Protons | Bacteria - metabolism | Animals | Oxidation-Reduction | Electron Transport - physiology | Mitochondria - physiology | Enzymes - metabolism | Cytochrome | Oxidoreductase | Metals | Cytochrome-c oxidase | Electron transfer | Chains | Crystallography | X-ray crystallography | Coupling (molecular) | Quinones | Mitochondria | Allosteric properties | Ubiquinone | NADH | Bacteria | Oxidation | Ubiquinone oxidoreductase | Catalysis | Translocation | Enzymes | Protonmotive force | Substrates | Equivalence | Nicotinamide adenine dinucleotide | Electron transport
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