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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 | Index Medicus | solar (fuels), biofuels (including algae and biomass), bio-inspired, hydrogen and fuel cells | Bioenergetics
Journal Article
Science, ISSN 0036-8075, 7/2008, Volume 321, Issue 5888, pp. 572 - 575
Journal Article
JOURNAL OF BIOLOGICAL CHEMISTRY, ISSN 0021-9258, 01/2016, Volume 291, Issue 3, pp. 1175 - 1197
The recent classification of glycoside hydrolase family 5 (GH5) members into subfamilies enhances the prediction of substrate specificity by phylogenetic... 
SUBSTRATE-SPECIFICITY | POLYSACCHARIDE LYASES | SITE NUCLEOPHILE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CARBOHYDRATE-ACTIVE ENZYMES | ENZYMATIC-HYDROLYSIS | XYLOGLUCAN | ENDOGLUCANASE GENE | MASS-SPECTROMETRY | CELL-WALLS | CLOSTRIDIUM-CELLULOLYTICUM | Cellulase - chemistry | Xylans - metabolism | Cellulase - antagonists & inhibitors | Cellulase - genetics | Endo-1,3-beta-Glucanase - chemistry | Glycoside Hydrolases - genetics | Bacterial Proteins - chemistry | Substrate Specificity | Endo-1,3-beta-Glucanase - antagonists & inhibitors | Phylogeny | Cellulose - chemistry | Cellulase - metabolism | Enzyme Inhibitors - chemistry | Apoenzymes - metabolism | Glycoside Hydrolases - chemistry | Glucans - metabolism | Apoenzymes - antagonists & inhibitors | Glycoside Hydrolases - antagonists & inhibitors | Recombinant Proteins - metabolism | Bacterial Proteins - antagonists & inhibitors | Catalytic Domain | Biocatalysis | Enzyme Inhibitors - metabolism | Bacterial Proteins - genetics | Enzyme Inhibitors - pharmacology | Endo-1,3-beta-Glucanase - metabolism | Models, Molecular | Recombinant Proteins - chemistry | Hot Temperature | Endo-1,3-beta-Glucanase - genetics | Xylans - chemistry | Apoenzymes - genetics | Apoenzymes - chemistry | Bacterial Proteins - metabolism | Protein Conformation | Glucans - chemistry | Glycoside Hydrolases - metabolism | Mutation | Prevotella - enzymology | Amino Acid Substitution | Cellulose - metabolism | Hydrogen-Ion Concentration | Index Medicus | Life Sciences | Biomolecules | Quantitative Methods | Biochemistry, Molecular Biology
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 35, pp. 14617 - 14624
Using the energy of ATP hydrolysis, ABC transporters catalyze the trans-membrane transport of molecules. In bacteria, these transporters partner with a... 
ANTHRACIS VIRULENCE DETERMINANT | MALTOSE TRANSPORT | BTUCD-F | MECHANISM | YERSINIA-PESTIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | CASSETTE TRANSPORTER | CRYSTAL-STRUCTURES | MULTIDRUG-RESISTANCE | HISTIDINE PERMEASE | Surface Plasmon Resonance | Hemeproteins - genetics | Heme - metabolism | Protein Multimerization | Bacterial Proteins - chemistry | Holoenzymes - chemistry | Recombinant Proteins | Cell Membrane - chemistry | ATP-Binding Cassette Transporters - chemistry | Holoenzymes - metabolism | ATP-Binding Cassette Transporters - genetics | Heme - chemistry | Adenosine Triphosphate - metabolism | Hemeproteins - chemistry | Apoenzymes - metabolism | ATP-Binding Cassette Transporters - metabolism | Carrier Proteins - chemistry | Receptors, Cell Surface - chemistry | Cell Membrane - metabolism | Protein Interaction Domains and Motifs | Dimerization | Immobilized Proteins - chemistry | Yersinia pestis - metabolism | Hemeproteins - metabolism | Immobilized Proteins - genetics | Bacterial Proteins - genetics | Models, Molecular | Receptors, Cell Surface - metabolism | Hydrolysis | Carrier Proteins - genetics | Carrier Proteins - metabolism | Apoenzymes - genetics | Immobilized Proteins - metabolism | Apoenzymes - chemistry | Bacterial Proteins - metabolism | Holoenzymes - genetics | Molecular Docking Simulation | Kinetics | Adenosine Triphosphate - chemistry | Receptors, Cell Surface - genetics | Index Medicus | Membrane Biology | ATPase | membrane protein | protein-protein interaction | surface plasmon resonance (SPR) | ABC transporter | ATP
Journal Article
Nature, ISSN 0028-0836, 08/2010, Volume 466, Issue 7309, pp. 935 - 940
Despite the success of genomics in identifying new essential bacterial genes, there is a lack of sustainable leads in antibacterial drug discovery to address... 
BREAKAGE-REUNION DOMAIN | B-PROTEIN | BAD BUGS | MECHANISM | COLI DNA GYRASE | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | FUSION PROTEIN | INFECTIOUS-DISEASES-SOCIETY | CLEAVAGE | Staphylococcus aureus - enzymology | Crystallography, X-Ray | Structure-Activity Relationship | Quinolines - pharmacology | Quinolones - chemistry | Anti-Bacterial Agents - chemistry | Topoisomerase II Inhibitors | Apoenzymes - metabolism | DNA, Superhelical - chemistry | Drug Design | Binding Sites | Ciprofloxacin - metabolism | Drug Resistance | Catalytic Domain | Escherichia coli - enzymology | DNA Gyrase - chemistry | Quinolines - chemistry | Quinolones - metabolism | Models, Molecular | Anti-Bacterial Agents - metabolism | DNA - metabolism | Quinolines - metabolism | DNA Gyrase - metabolism | DNA - chemistry | Manganese - metabolism | Apoenzymes - chemistry | Ciprofloxacin - chemistry | Aspartic Acid - metabolism | Protein Conformation | Anti-Bacterial Agents - pharmacology | DNA, Superhelical - metabolism | Arginine - metabolism | DNA Cleavage | Antimitotic agents | Enzymes | Drug resistance in microorganisms | Topoisomerases | DNA | Genes | Research | Properties | Antineoplastic agents | Antibacterial agents | Staphylococcus aureus | Bacteria | Mutation | E coli | Deoxyribonucleic acid--DNA | Streptococcus infections | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 32, pp. 13154 - 13167
In many Gram-negative bacteria, including Rhodobacter capsulatus, cytochrome c maturation (Ccm) is carried out by a membrane-integral machinery composed of... 
SYSTEM | NULL MUTANTS | PROTEIN | APOCYTOCHROME-C | BIOGENESIS DEFECT | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI CCMG | THIOREDOXIN REDUCTASE | CATALYTIC MECHANISM | DISULFIDE | RHODOBACTER-CAPSULATUS | Heme - metabolism | Stereoisomerism | Protein Multimerization | Bacterial Proteins - chemistry | Recombinant Fusion Proteins - metabolism | Cystine - chemistry | Cytochromes c - chemistry | Apoenzymes - metabolism | Cysteine - metabolism | Protein Interaction Domains and Motifs | Binding Sites | Peptide Fragments - genetics | Bacterial Outer Membrane Proteins - genetics | Protein Disulfide Reductase (Glutathione) - metabolism | Recombinant Proteins - metabolism | Peptide Fragments - metabolism | Oxidation-Reduction | Rhodobacter capsulatus - enzymology | Cytochromes c - metabolism | Bacterial Proteins - genetics | Bacterial Outer Membrane Proteins - chemistry | Recombinant Proteins - chemistry | Cysteine - chemistry | Recombinant Fusion Proteins - chemistry | Protein Disulfide Reductase (Glutathione) - chemistry | Peptide Fragments - chemistry | Protein Disulfide Reductase (Glutathione) - genetics | Bacterial Outer Membrane Proteins - metabolism | Models, Biological | Cystine - metabolism | Apoenzymes - chemistry | Bacterial Proteins - metabolism | Mutation | Amino Acid Substitution | Index Medicus | Life Sciences | Biochemistry, Molecular Biology | Biochemistry & Molecular Biology | thiol | Rhodobacter capsulatus | cytochrome c maturation | thiol–disulfide exchange | Bioenergetics | disulfide | heme | thioreduction | protein–protein interaction | apocytochrome | cytochrome c
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 32, pp. 13323 - 13332
Polycomb-group proteins control many fundamental biological processes, such as anatomical development in mammals and vernalization in plants. Polycomb... 
METHYLATION | PRC2 | RNA | HISTONE H3 | METHYLTRANSFERASES | BIOCHEMISTRY & MOLECULAR BIOLOGY | MUTATION | MARKS | H3K27ME3 | GAIN | EZH2 | Fungal Proteins - chemistry | Polycomb Repressive Complex 2 - genetics | Histones - chemistry | S-Adenosylmethionine - chemistry | Recombinant Fusion Proteins - metabolism | Xenopus Proteins - chemistry | Coenzymes - metabolism | Apoenzymes - metabolism | Conserved Sequence | Lysine - metabolism | Protein Interaction Domains and Motifs | Coenzymes - chemistry | Peptide Fragments - genetics | Enhancer of Zeste Homolog 2 Protein - chemistry | Amino Acid Sequence | Enhancer of Zeste Homolog 2 Protein - genetics | Enhancer of Zeste Homolog 2 Protein - metabolism | Peptide Fragments - metabolism | Models, Molecular | Chaetomium - enzymology | Fungal Proteins - genetics | Recombinant Fusion Proteins - chemistry | Polycomb Repressive Complex 2 - chemistry | Peptide Fragments - chemistry | Animals | Xenopus laevis - metabolism | Apoenzymes - genetics | Apoenzymes - chemistry | Xenopus Proteins - metabolism | Protein Processing, Post-Translational | Histones - metabolism | Mutation | Methylation | Polycomb Repressive Complex 2 - metabolism | S-Adenosylmethionine - metabolism | Amino Acid Substitution | Fungal Proteins - metabolism | Index Medicus | enzyme | crystal structure | Protein Structure and Folding | histone methylation | epigenetics | polycomb
Journal Article
Biochemistry, ISSN 0006-2960, 10/2017, Volume 56, Issue 41, pp. 5593 - 5603
Journal Article
Journal Article
Biochemistry, ISSN 0006-2960, 11/2013, Volume 52, Issue 47, pp. 8430 - 8441
Tyrosine hydroxylase is a nonheme iron enzyme found in the nervous system that catalyzes the hydroxylation of tyrosine to form L-3,4-dihydroxyphenylalanine,... 
IRON-NITROSYL COMPLEXES | ISOPENICILLIN-N-SYNTHASE | ANGSTROM RESOLUTION | ACTIVE-SITE IRON | POINT MUTATION | O-2 ACTIVATION | CRYSTAL-STRUCTURE | TRYPTOPHAN-HYDROXYLASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROTOCATECHUATE 4,5-DIOXYGENASE | ENVELOPE MODULATION SPECTROSCOPY | Deuterium | Tyrosine 3-Monooxygenase - metabolism | Pterins - metabolism | Humans | Molecular Conformation | Quaternary Ammonium Compounds - chemistry | Nerve Tissue Proteins - chemistry | Tyrosine 3-Monooxygenase - chemistry | Apoenzymes - metabolism | Ferrous Compounds - chemistry | Pterins - chemistry | Tyrosine - chemistry | Recombinant Proteins - metabolism | Catalytic Domain | Biocatalysis | Electron Spin Resonance Spectroscopy | Hydroxylation | Nitric Oxide - chemistry | Oxidation-Reduction | Iron - chemistry | Recombinant Proteins - chemistry | Mutant Proteins - metabolism | Iron - metabolism | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Tyrosine 3-Monooxygenase - genetics | Tyrosine - metabolism | Apoenzymes - genetics | Mutant Proteins - chemistry | Ferrous Compounds - metabolism | Quaternary Ammonium Compounds - metabolism | Apoenzymes - chemistry | Protein Binding | Nitric Oxide - metabolism | Amino Acid Substitution | Amino acids | Chemical properties | Research | Metalloproteins | Nitric oxide | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/2017, Volume 292, Issue 34, pp. 14026 - 14038
Hydrogen sulfide (H2S) is a signaling molecule that is toxic at elevated concentrations. In eukaryotes, it is cleared via a mitochondrial sulfide oxidation... 
LIVER RHODANESE | SULFURTRANSFERASE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | H2S | HYDROGEN-SULFIDE | enzyme kinetics | X-ray crystallography | hydrogen sulfide | ETHE1 | iron | sulfur | STAPHYLOCOCCUS-AUREUS | MUTATIONS | ELECTROSTATICS | ETHYLMALONIC ENCEPHALOPATHY | Disulfides - metabolism | Hydrogen Sulfide - metabolism | Burkholderiaceae - enzymology | Glutathione - metabolism | Mutant Chimeric Proteins - genetics | Thiosulfate Sulfurtransferase - genetics | Bacterial Proteins - chemistry | Crystallography, X-Ray | Mutant Chimeric Proteins - chemistry | Thiosulfate Sulfurtransferase - chemistry | Quinone Reductases - chemistry | Thiosulfate Sulfurtransferase - metabolism | Mutant Chimeric Proteins - metabolism | Apoenzymes - metabolism | Peptide Fragments - genetics | Recombinant Proteins - metabolism | Quinone Reductases - metabolism | Catalytic Domain | Peptide Fragments - metabolism | Biocatalysis | Glutathione - analogs & derivatives | Bacterial Proteins - genetics | Computational Biology | Enzyme Stability | Models, Molecular | Recombinant Proteins - chemistry | Cysteine - chemistry | Thiosulfates - metabolism | Peptide Fragments - chemistry | Apoenzymes - genetics | Apoenzymes - chemistry | Bacterial Proteins - metabolism | Protein Conformation | Quinone Reductases - genetics | Glutathione - chemistry | Mutation | Amino Acid Substitution | Index Medicus | BASIC BIOLOGICAL SCIENCES | Enzymology
Journal Article
Biochemistry, ISSN 0006-2960, 07/2017, Volume 56, Issue 27, pp. 3443 - 3453
CTX-M beta-lactamases provide resistance against the beta-lactam antibiotic, cefotaxime, but not a related antibiotic, ceftazidime. beta-Lactamases that carry... 
M ENZYMES | ANGSTROM RESOLUTION | SUBSTITUTION | EXTENDED-SPECTRUM | OMEGA-LOOP | CATALYTIC-PROPERTIES | GLOBAL SUPPRESSOR | BIOCHEMISTRY & MOLECULAR BIOLOGY | HYDROLYSIS | CEFTAZIDIME RESISTANCE | PEPTIDE-BOND | Ceftazidime - pharmacology | Escherichia coli - drug effects | Cephalosporins - chemistry | Substrate Specificity | Crystallography, X-Ray | Ceftazidime - metabolism | beta-Lactamases - genetics | Oximes - metabolism | Anti-Bacterial Agents - chemistry | Drug Resistance, Multiple, Bacterial | Apoenzymes - metabolism | Ceftazidime - chemistry | beta-Lactamases - metabolism | Cephalosporins - pharmacology | Acylation | Recombinant Proteins - metabolism | Catalytic Domain | Escherichia coli - enzymology | Mutagenesis, Site-Directed | Enzyme Stability | Models, Molecular | Recombinant Proteins - chemistry | Anti-Bacterial Agents - metabolism | Escherichia coli Proteins - metabolism | Hydrolysis | Oximes - chemistry | Point Mutation | beta-Lactamases - chemistry | Apoenzymes - genetics | Apoenzymes - chemistry | Escherichia coli Proteins - genetics | Oximes - pharmacology | Ligands | Protein Conformation | Anti-Bacterial Agents - pharmacology | Escherichia coli Proteins - chemistry | Amino Acid Substitution | Cephalosporins - metabolism | Moxalactam | Cephalosporins | Analysis | Beta lactamases | Cephaloridine | Research | Index Medicus | INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
Journal Article
Journal Article
Biochemistry, ISSN 0006-2960, 10/2017, Volume 56, Issue 41, pp. 5539 - 5549
Journal Article
FEBS Journal, ISSN 1742-464X, 09/2015, Volume 282, Issue 17, pp. 3412 - 3423
The genome of some methanogens contains besides the [Fe]‐hydrogenase (Hmd) a related protein termed Hmd II . We showed by X‐ray and infrared spectroscopic data... 
methanogenic archaea | tetrahydromethanopterin | [Fe]‐hydrogenase | sensor protein | Hmd paralogs | [Fe]-hydrogenase | ACTIVE-SITE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | INFRARED-SPECTROSCOPY | H-2 ACTIVATION | CLUSTER-FREE HYDROGENASE | COMPLETE GENOME SEQUENCE | H-2-FORMING METHYLENETETRAHYDROMETHANOPTERIN DEHYDROGENASE | TRANSFER-RNA SYNTHETASE | ACYL-IRON LIGATION | Pterins - metabolism | Hydrogenase - genetics | Pyridines - chemistry | Archaeal Proteins - chemistry | Iron-Sulfur Proteins - genetics | Crystallography, X-Ray | Holoenzymes - chemistry | Hydrogenase - chemistry | Iron-Sulfur Proteins - chemistry | Coenzymes - metabolism | Hydrogenase - metabolism | Holoenzymes - metabolism | Spectrophotometry, Infrared | Apoenzymes - metabolism | Escherichia coli - metabolism | Archaeal Proteins - genetics | Protein Biosynthesis - genetics | Protein Interaction Domains and Motifs | Pterins - chemistry | Coenzymes - chemistry | Binding Sites | Methanocaldococcus - chemistry | Archaeal Proteins - metabolism | Recombinant Proteins - metabolism | Gene Expression | Protein Structure, Secondary | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Protein Folding | Pyridines - metabolism | Escherichia coli - genetics | Apoenzymes - genetics | Methanocaldococcus - enzymology | Apoenzymes - chemistry | Protein Binding | Holoenzymes - genetics | Iron-Sulfur Proteins - metabolism | Kinetics | Physiological aspects | Protein biosynthesis | Sensors | Aminoacyl-tRNA synthetases | Analysis | Transfer RNA | Enzymes | Biophysics | Protein synthesis | Index Medicus
Journal Article