tyrosine and flavin-adenine dinucleotide

tyrosine has been researched along with flavin-adenine dinucleotide in 54 studies

Research

Studies (54)

TimeframeStudies, this research(%)All Research%
pre-199010 (18.52)18.7374
1990's8 (14.81)18.2507
2000's20 (37.04)29.6817
2010's14 (25.93)24.3611
2020's2 (3.70)2.80

Authors

AuthorsStudies
Kasper, CB; Porter, TD; Shen, AL; Wilson, TE1
Hayaishi, O; Nozaki, M1
Veeger, C; Visser, J1
de Wit, JL; Grande, HJ; Müller, F; Veeger, C; Visser, AJ1
Edmondson, DE; Kenney, WC; Singer, TP1
Kearney, EB; Seng, R; Singer, TP; Walker, WH1
MacKenzie, RE; McCormick, DB; Wu, FY1
McCormick, DB; Ying-Hsiueh Wu, F1
Bright, HJ; Porter, DJ1
Calcaterra, NB; Carrillo, N; Ceccarelli, EA; Orellano, EG; Ottado, J; Picó, GA1
Abell, CW; Kirksey, TJ; Kwan, SW; Lewis, DA; Zhou, BP1
Covès, J; Eschenbrenner, M; Fontecave, M; Nivière, V1
Benson, TE; Hogle, JM; Walsh, CT1
Hille, R; Huang, L; Mathews, FS; Scrutton, NS; Sutcliffe, MJ; Wilson, EK1
Aubert, C; Brettel, K; Eker, AP; Mathis, P1
Carey, PR; Dong, J; Palfey, BA; Zheng, Y1
Kanadia, RN; Kuo, WN; Shanbhag, VP; Toro, R1
Banerjee, A; Fitzpatrick, PF; Gadda, G1
Dou, Y; Gardner, AM; Gardner, PR; Martin, LA; Olson, JS1
Cronin, CN; Efimov, I; McIntire, WS1
Becker, DF; Fuchs, JA; Pellett, JD; Saenger, AK; Stankovich, MT1
Aeschliman, SM; Ballou, DP; Massey, V; Ortiz-Maldonado, M1
Iyanagi, T; Kimura, S; Nishida, H1
Ito, A; Ma, J1
Arruda, P; Castro, GM; de Nucci, G; Langone, F; Martins, ML; Muscará, MN; Papes, F; Rogério, F; Santos, LM; Teixeira, SA1
Liu, YY; Lu, CY1
Ahmad, M; Brettel, K; Byrdin, M; Giovani, B1
Bauer, CE; Dragnea, V; Kikuchi, J; Kraft, BJ; Masuda, S; Tollin, G; Zaleski, JM1
ICHIKAWA, Y; YAMANO, T1
Orrit, M1
Cova, S; Karnchanaphanurach, P; Louie, TM; Luo, G; Rech, I; Xie, XS; Xun, L; Yang, H1
Kou, SC; Xie, XS1
Barber, MJ; Crowley, LJ; Davis, CA; Marohnic, CC; Smith, ET1
Frago, S; Gómez-Moreno, C; Martínez-Júlvez, M; Medina, M; Nogués, I; Peregrina, JR; Tejero, J1
Basran, J; Fullerton, S; Leys, D; Scrutton, NS1
Aliverti, A; Carpanelli, E; Coda, A; Mattevi, A; Mattiroli, F; Pandini, V; Razeto, A1
Li, D; Liu, Y; Wu, L; Zeng, J1
Fukushima, Y; Ikeuchi, M; Itoh, S; Murai, Y; Okajima, K1
Chen, CL; Chen, YR; Garg, V; Green-Church, KB; Hu, K; Kang, PT; Zhang, L1
Daggett, V; Merkley, ED; Parson, WW1
Aalders, MC; de Vos, J; Lambrechts, SA; Sijen, T; van Dam, A; van Weert, A1
Arai, S; Blaber, M; Kurihara, K; Kuroki, R; Morimoto, S; Shoyama, Y; Takeuchi, A; Tamada, T; Taura, F1
Biskup, T; Getzoff, ED; Hitomi, K; Okafuji, A; Paulus, B; Schleicher, E; Weber, S1
Elstner, M; Kubař, T; Lüdemann, G; Steinbrecher, TB; Woiczikowski, PB1
Alsaeed, AH; AlSalhi, MS; Devanesan, S; Ganesh, KM; Masilamani, V; Palled, S; Perinbam, K; Prasad, S; Ravikumar, M1
Naito, H; Nishimura, E; Sakurai, T; Seo, D1
Bou-Nader, C; Cornu, D; Fontecave, M; Hamdane, D; Hui-Bon-Hoa, G1
Aprodu, I; Dumitrașcu, L; Stănciuc, N1
Brust, R; French, JB; Gil, AA; Greetham, GM; Hall, CR; Iuliano, JN; Laptenok, SP; Lukacs, A; Meech, SR; Tonge, PJ; Towrie, M; Verma, A; Yoon, GE1
Deng, S; Li, P; Wang, Y; Zeng, J1
Bou-Nader, C; Dozova, N; Hamdane, D; Lacombat, F; Plaza, P1
Lukacs, A; Nag, L; Vos, MH1
Imamoto, Y; Mitsui, H; Miura, K; Okano, K; Okano, T; Otsuka, H1
Beck, S; Domratcheva, T; Hegemann, P; Hontani, Y; Kennis, JTM; Kloz, M; Mathes, T; Mehlhorn, J1

Other Studies

54 other study(ies) available for tyrosine and flavin-adenine dinucleotide

ArticleYear
Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed mutagenesis.
    The Journal of biological chemistry, 1989, May-05, Volume: 264, Issue:13

    Topics: Amino Acid Sequence; Animals; Base Sequence; Catalysis; Cloning, Molecular; Cytochrome P-450 Enzyme System; DNA Mutational Analysis; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Kinetics; Molecular Sequence Data; NADH Dehydrogenase; NADP; NADPH-Ferrihemoprotein Reductase; Oxidoreductases; Rats; Spectrum Analysis; Tyrosine

1989
Nature and mechanisms of oxygenases.
    Science (New York, N.Y.), 1969, Apr-25, Volume: 164, Issue:3878

    Topics: Amino Acids; Bacteria; Biotransformation; Catalysis; Catechol Oxidase; Chemical Phenomena; Chemistry; Cholesterol; Collagen; Dihydroxyphenylalanine; Flavin-Adenine Dinucleotide; Hydroxyproline; Lysine; NAD; Oxygen; Oxygenases; Phenylalanine; Plants; Prostaglandins; Squalene; Tryptophan Oxygenase; Tyrosine

1969
Relation between conformations and activities of lipoamide dehydrogenase. IV. Apoenzyme structure and flavin binding aspects.
    Biochimica et biophysica acta, 1970, May-13, Volume: 206, Issue:2

    Topics: Adenine; Binding Sites; Chemical Phenomena; Chemistry; Chloromercuribenzoates; Cold Temperature; Dihydrolipoamide Dehydrogenase; Diphosphates; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavins; Fluorometry; Halogens; Hot Temperature; Hydrogen-Ion Concentration; Osmolar Concentration; Protein Binding; Protein Denaturation; Time Factors; Tryptophan; Tyrosine; Urea

1970
Spin label studies on the flavoproteins lipoamide dehydrogenase and D-amino acid oxidase.
    Zeitschrift fur Naturforschung. Teil B. Anorganische Chemie, organische Chemie, Biochemie, Biophysik, Biologie, 1972, Volume: 27, Issue:9

    Topics: Alanine; Binding Sites; D-Amino-Acid Oxidase; Dihydrolipoamide Dehydrogenase; Electron Spin Resonance Spectroscopy; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Maleimides; Protein Conformation; Temperature; Tyrosine; Urea

1972
The covalently bound flavin of Chromatium cytochrome c552. 2. Sequence of flavin peptides and flavin-tyrosine interaction.
    European journal of biochemistry, 1974, Oct-02, Volume: 48, Issue:2

    Topics: Amino Acid Sequence; Amino Acids; Binding Sites; Chromatium; Circular Dichroism; Cytochromes; Flavin-Adenine Dinucleotide; Flavins; Oxidation-Reduction; Protein Binding; Spectrometry, Fluorescence; Tyrosine

1974
Sequence and structure of a cysteinyl flavin peptide from monoamine oxidase.
    Biochemical and biophysical research communications, 1971, Jul-16, Volume: 44, Issue:2

    Topics: Amino Acid Sequence; Aminopeptidases; Binding Sites; Chromatography, Paper; Cysteine; Electrophoresis, Paper; Flavin-Adenine Dinucleotide; Fluorometry; Formates; Glycine; Hydrolysis; Indicators and Reagents; Liver; Monoamine Oxidase; Oxidation-Reduction; Peptides; Protein Binding; Serine; Spectrophotometry; Tyrosine

1971
Kinetics and mechanism of oxidation-reduction reactions between pyridine nucleotides and flavins.
    Biochemistry, 1970, May-26, Volume: 9, Issue:11

    Topics: Alanine; Amino Acids; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavins; Hot Temperature; Hydrocarbons; Kinetics; Nucleotides; Oxidation-Reduction; Peptides; Phenylalanine; Pyridines; Tryptophan; Tyrosine

1970
Flavin-sensitized photooxidations of tryptophan and tyrosine.
    Biochimica et biophysica acta, 1971, May-25, Volume: 236, Issue:2

    Topics: Acetates; Colorimetry; Dimethyl Sulfoxide; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavins; Hydrogen-Ion Concentration; Kinetics; Light; Oxidation-Reduction; Peptides; Photochemistry; Radiation Effects; Temperature; Tryptophan; Tyrosine

1971
Location of hydrogen transfer steps in the mechanism of reduction of L-amino acid oxidase.
    Biochemical and biophysical research communications, 1969, Jul-23, Volume: 36, Issue:2

    Topics: Amino Acid Oxidoreductases; Chemical Phenomena; Chemistry; Deuterium; Flavin-Adenine Dinucleotide; Glycine; Hydrogen; Kinetics; Phenylalanine; Spectrophotometry; Tritium; Tyrosine

1969
Contribution of the FAD binding site residue tyrosine 308 to the stability of pea ferredoxin-NADP+ oxidoreductase.
    Biochemistry, 1995, Oct-03, Volume: 34, Issue:39

    Topics: Binding Sites; Enzyme Stability; Ferredoxin-NADP Reductase; Flavin-Adenine Dinucleotide; Hot Temperature; Mutation; Pisum sativum; Protein Denaturation; Spectrometry, Fluorescence; Tyrosine

1995
Mutagenesis at a highly conserved tyrosine in monoamine oxidase B affects FAD incorporation and catalytic activity.
    Biochemistry, 1995, Jul-25, Volume: 34, Issue:29

    Topics: Amino Acid Sequence; Animals; Arabidopsis; Base Sequence; Binding Sites; Cell Line; Chlorocebus aethiops; Conserved Sequence; Escherichia coli; Flavin-Adenine Dinucleotide; Humans; Kidney; Kinetics; Models, Structural; Molecular Sequence Data; Monoamine Oxidase; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Point Mutation; Protein Conformation; Rats; Recombinant Proteins; Sequence Homology, Amino Acid; Spinacia oleracea; Transfection; Tyrosine

1995
NADPH-sulfite reductase from Escherichia coli. A flavin reductase participating in the generation of the free radical of ribonucleotide reductase.
    The Journal of biological chemistry, 1993, Sep-05, Volume: 268, Issue:25

    Topics: Amino Acid Sequence; Blotting, Western; Catalysis; Electron Transport; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; FMN Reductase; Free Radicals; Hydroxyurea; Molecular Sequence Data; Molecular Weight; Mutation; NADH, NADPH Oxidoreductases; NADP; Oxidoreductases Acting on Sulfur Group Donors; Ribonucleotide Reductases; Sulfite Reductase (NADPH); Tyrosine

1993
The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls.
    Structure (London, England : 1993), 1996, Jan-15, Volume: 4, Issue:1

    Topics: Bacterial Proteins; Binding Sites; Carbohydrate Dehydrogenases; Cell Wall; Crystallography, X-Ray; Flavin-Adenine Dinucleotide; Hydrogen Bonding; Models, Chemical; Models, Molecular; Molecular Structure; NADP; Oxidation-Reduction; Protein Binding; Protein Conformation; Tyrosine; Uridine Diphosphate N-Acetylglucosamine

1996
An exposed tyrosine on the surface of trimethylamine dehydrogenase facilitates electron transfer to electron transferring flavoprotein: kinetics of transfer in wild-type and mutant complexes.
    Biochemistry, 1997, Jan-07, Volume: 36, Issue:1

    Topics: Bacteria; Binding Sites; Coloring Agents; Electron Transport; Flavin-Adenine Dinucleotide; Flavoproteins; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Oxidoreductases, N-Demethylating; Spectrophotometry; Tyrosine

1997
Intraprotein electron transfer between tyrosine and tryptophan in DNA photolyase from Anacystis nidulans.
    Proceedings of the National Academy of Sciences of the United States of America, 1999, May-11, Volume: 96, Issue:10

    Topics: Cyanobacteria; Deoxyribodipyrimidine Photo-Lyase; Electron Transport; Escherichia coli; Flavin-Adenine Dinucleotide; Free Radicals; Kinetics; Lasers; Light; Mercaptoethanol; Oxidation-Reduction; Recombinant Proteins; Tryptophan; Tyrosine

1999
Using Raman spectroscopy to monitor the solvent-exposed and "buried" forms of flavin in p-hydroxybenzoate hydroxylase.
    Biochemistry, 1999, Dec-21, Volume: 38, Issue:51

    Topics: 4-Hydroxybenzoate-3-Monooxygenase; Amino Acid Substitution; Binding Sites; Flavin-Adenine Dinucleotide; Flavins; Mutagenesis, Site-Directed; Phenylalanine; Protein Conformation; Pseudomonas aeruginosa; Solvents; Spectrum Analysis, Raman; Tyrosine

1999
Denitration of peroxynitrite-treated proteins by 'protein nitratases' from rat brain and heart.
    Molecular and cellular biochemistry, 1999, Volume: 201, Issue:1-2

    Topics: Animals; beta-Fructofuranosidase; Blotting, Western; Brain; Brain Chemistry; Calcium; Dialysis; Enzymes; Flavin-Adenine Dinucleotide; Glutathione; Glutathione Transferase; Glycoside Hydrolases; Myocardium; NAD; NADP; Nitrates; Proteins; Rats; Serum Albumin, Bovine; Tissue Extracts; Tyrosine

1999
Identification of an essential tyrosine residue in nitroalkane oxidase by modification with tetranitromethane.
    Biochemistry, 2000, Feb-08, Volume: 39, Issue:5

    Topics: Amino Acid Sequence; Binding Sites; Dioxygenases; Enzyme Activation; Enzyme Inhibitors; Flavin-Adenine Dinucleotide; Fusarium; Indicators and Reagents; Kinetics; Molecular Sequence Data; Oxygenases; Tetranitromethane; Tyrosine

2000
Steady-state and transient kinetics of Escherichia coli nitric-oxide dioxygenase (flavohemoglobin). The B10 tyrosine hydroxyl is essential for dioxygen binding and catalysis.
    The Journal of biological chemistry, 2000, Apr-28, Volume: 275, Issue:17

    Topics: Amino Acids; Dose-Response Relationship, Drug; Escherichia coli; Flavin-Adenine Dinucleotide; Kinetics; Ligands; Models, Biological; Mutagenesis; NADP; Nitric Oxide; Oxidation-Reduction; Oxygen; Oxygenases; Time Factors; Tyrosine

2000
Effects of noncovalent and covalent FAD binding on the redox and catalytic properties of p-cresol methylhydroxylase.
    Biochemistry, 2001, Feb-20, Volume: 40, Issue:7

    Topics: Amino Acid Substitution; Binding Sites; Catalysis; Cytochromes; Flavin-Adenine Dinucleotide; Flavoproteins; Mixed Function Oxygenases; Mutagenesis, Site-Directed; Oxidation-Reduction; Phenylalanine; Pseudomonas putida; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Tyrosine

2001
Role of aromatic stacking interactions in the modulation of the two-electron reduction potentials of flavin and substrate/product in Megasphaera elsdenii short-chain acyl-coenzyme A dehydrogenase.
    Biochemistry, 2001, Jun-26, Volume: 40, Issue:25

    Topics: Acyl Coenzyme A; Acyl-CoA Dehydrogenase; Binding Sites; Catalysis; Electrochemistry; Electron Transport; Fatty Acid Desaturases; Flavin-Adenine Dinucleotide; Macromolecular Substances; Mutagenesis, Site-Directed; Oxidation-Reduction; Peptostreptococcus; Phenylalanine; Recombinant Proteins; Spectrometry, Fluorescence; Substrate Specificity; Thermodynamics; Tryptophan; Tyrosine

2001
Synergistic interactions of multiple mutations on catalysis during the hydroxylation reaction of p-hydroxybenzoate hydroxylase: studies of the Lys297Met, Asn300Asp, and Tyr385Phe mutants reconstituted with 8-Cl-flavin.
    Biochemistry, 2001, Jul-31, Volume: 40, Issue:30

    Topics: 4-Hydroxybenzoate-3-Monooxygenase; Alanine; Amino Acid Substitution; Anaerobiosis; Asparagine; Aspartic Acid; Catalysis; Flavin-Adenine Dinucleotide; Hydroxylation; Lysine; Methionine; Mutagenesis, Site-Directed; Oxidation-Reduction; Parabens; Phenylalanine; Riboflavin; Serine; Spectrophotometry; Substrate Specificity; Tyrosine

2001
Effects of flavin-binding motif amino acid mutations in the NADH-cytochrome b5 reductase catalytic domain on protein stability and catalysis.
    Journal of biochemistry, 2001, Volume: 130, Issue:4

    Topics: Amino Acid Motifs; Animals; Arginine; Binding Sites; Catalysis; Catalytic Domain; Circular Dichroism; Cytochrome Reductases; Cytochrome-B(5) Reductase; Enzyme Stability; Flavin-Adenine Dinucleotide; Kinetics; Models, Chemical; Mutation; NAD; Protein Binding; Protein Denaturation; Protein Structure, Tertiary; Serine; Swine; Tyrosine

2001
Tyrosine residues near the FAD binding site are critical for FAD binding and for the maintenance of the stable and active conformation of rat monoamine oxidase A.
    Journal of biochemistry, 2002, Volume: 131, Issue:1

    Topics: Amino Acid Sequence; Animals; Binding Sites; Cysteine; Enzyme Stability; Flavin-Adenine Dinucleotide; Humans; Kinetics; Molecular Sequence Data; Monoamine Oxidase; Point Mutation; Protein Conformation; Rats; Substrate Specificity; Tyrosine; Yeasts

2002
Expression and activity of nitric oxide synthase isoforms in rat brain during the development of experimental allergic encephalomyelitis.
    Brain research. Molecular brain research, 2002, Feb-28, Volume: 99, Issue:1

    Topics: Animals; Biopterins; Brain; Calcium; Calmodulin; Disease Models, Animal; Disease Progression; Encephalomyelitis, Autoimmune, Experimental; Female; Flavin-Adenine Dinucleotide; Male; NADP; Neurons; Nitric Oxide; Nitric Oxide Synthase; Protein Isoforms; Rats; Rats, Inbred Lew; RNA, Messenger; Subcellular Fractions; Tyrosine

2002
Electron transfer oxidation of tryptophan and tyrosine by triplet states and oxidized radicals of flavin sensitizers: a laser flash photolysis study.
    Biochimica et biophysica acta, 2002, May-10, Volume: 1571, Issue:1

    Topics: Electron Transport; Flavin-Adenine Dinucleotide; Free Radicals; Lasers; Photochemistry; Photolysis; Riboflavin; Tryptophan; Tyrosine

2002
Light-induced electron transfer in a cryptochrome blue-light photoreceptor.
    Nature structural biology, 2003, Volume: 10, Issue:6

    Topics: Arabidopsis Proteins; Cryptochromes; Drosophila Proteins; Electron Transport; Eye Proteins; Flavin-Adenine Dinucleotide; Flavoproteins; Kinetics; Light; Photoreceptor Cells, Invertebrate; Receptors, G-Protein-Coupled; Spectrum Analysis; Tryptophan; Tyrosine

2003
Spectroscopic and mutational analysis of the blue-light photoreceptor AppA: a novel photocycle involving flavin stacking with an aromatic amino acid.
    Biochemistry, 2003, Jun-10, Volume: 42, Issue:22

    Topics: Amino Acid Sequence; Bacterial Proteins; Circular Dichroism; Flavin-Adenine Dinucleotide; Flavoproteins; Fluorescence; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Mutagenesis, Site-Directed; Photochemistry; Photolysis; Protein Binding; Protein Structure, Tertiary; Sequence Alignment; Sequence Homology, Amino Acid; Spectrophotometry, Ultraviolet; Tyrosine

2003
STUDIES ON THE PHOTOINACTIVATION OF D-AMINOACID OXIDASE.
    The Tokushima journal of experimental medicine, 1963, Volume: 10

    Topics: Chemical Phenomena; Chemistry; Coloring Agents; D-Amino-Acid Oxidase; Diphosphates; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Glutathione; Histidine; Hydrogen-Ion Concentration; Light; Methylene Blue; Oxidoreductases; Riboflavin; Sulfhydryl Compounds; Temperature; Tryptophan; Tyrosine

1963
Chemistry. The motions of an enzyme soloist.
    Science (New York, N.Y.), 2003, Oct-10, Volume: 302, Issue:5643

    Topics: Catalysis; Chemical Phenomena; Chemistry, Physical; Electrons; Escherichia coli; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavins; Fluorescence; FMN Reductase; Hydrogen Bonding; Lasers; Likelihood Functions; Mathematics; Mutation; Photons; Protein Conformation; Serine; Spectrometry, Fluorescence; Temperature; Thermodynamics; Tyrosine

2003
Protein conformational dynamics probed by single-molecule electron transfer.
    Science (New York, N.Y.), 2003, Oct-10, Volume: 302, Issue:5643

    Topics: Amino Acid Substitution; Catalysis; Chemical Phenomena; Chemistry, Physical; Computer Simulation; Electrons; Escherichia coli; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Flavins; Fluorescence; FMN Reductase; Hydrogen Bonding; Likelihood Functions; Mathematics; Models, Molecular; Mutagenesis, Site-Directed; Photons; Protein Conformation; Serine; Spectrometry, Fluorescence; Temperature; Thermodynamics; Tyrosine

2003
Generalized Langevin equation with fractional Gaussian noise: subdiffusion within a single protein molecule.
    Physical review letters, 2004, Oct-29, Volume: 93, Issue:18

    Topics: Flavin-Adenine Dinucleotide; Fluorescence; FMN Reductase; Models, Chemical; Models, Molecular; Protein Conformation; Tyrosine

2004
Cytochrome b5 reductase: role of the si-face residues, proline 92 and tyrosine 93, in structure and catalysis.
    Biochemistry, 2005, Feb-22, Volume: 44, Issue:7

    Topics: Amino Acid Motifs; Amino Acid Substitution; Animals; Catalysis; Circular Dichroism; Cytochrome-B(5) Reductase; Enzyme Activation; Flavin-Adenine Dinucleotide; Flavins; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Mutagenesis, Site-Directed; Oxidation-Reduction; Potentiometry; Proline; Rats; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Thermodynamics; Tyrosine

2005
Towards a new interaction enzyme:coenzyme.
    Biophysical chemistry, 2005, Apr-01, Volume: 115, Issue:2-3

    Topics: Anabaena; Apoenzymes; Ferredoxin-NADP Reductase; Flavin-Adenine Dinucleotide; Kinetics; Mutation; NADP; Oxidation-Reduction; Spectrum Analysis; Tyrosine

2005
Mechanism of FAD reduction and role of active site residues His-225 and Tyr-259 in Arthrobacter globiformis dimethylglycine oxidase: analysis of mutant structure and catalytic function.
    Biochemistry, 2006, Sep-19, Volume: 45, Issue:37

    Topics: Arthrobacter; Binding Sites; Catalysis; Flavin-Adenine Dinucleotide; Histidine; Models, Chemical; Models, Molecular; Molecular Structure; Mutant Proteins; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Tyrosine

2006
The crucial step in ether phospholipid biosynthesis: structural basis of a noncanonical reaction associated with a peroxisomal disorder.
    Structure (London, England : 1993), 2007, Volume: 15, Issue:6

    Topics: Alkyl and Aryl Transferases; Amino Acid Sequence; Amino Acid Substitution; Animals; Binding Sites; Catalysis; Chondrodysplasia Punctata, Rhizomelic; Conserved Sequence; Crystallography, X-Ray; Dictyostelium; Dimerization; Flavin-Adenine Dinucleotide; Histidine; Humans; Hydrogen Bonding; Lipid Metabolism, Inborn Errors; Models, Biological; Models, Chemical; Models, Molecular; Molecular Sequence Data; Molecular Structure; Peroxisomal Disorders; Phenylalanine; Phospholipid Ethers; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Recombinant Proteins; Sequence Homology, Amino Acid; Spectrum Analysis, Raman; Substrate Specificity; Tyrosine

2007
Mutation of Tyr375 to Lys375 allows medium-chain acyl-CoA dehydrogenase to acquire acyl-CoA oxidase activity.
    Biochimica et biophysica acta, 2007, Volume: 1774, Issue:12

    Topics: Acyl-CoA Dehydrogenase; Acyl-CoA Oxidase; Amino Acid Substitution; Animals; Base Sequence; Catalytic Domain; Coenzymes; Flavin-Adenine Dinucleotide; Liver; Lysine; Models, Biological; Models, Molecular; Mutagenesis, Site-Directed; Mutant Proteins; Mutation; Rats; Substrate Specificity; Tyrosine

2007
Photoreactions of Tyr8- and Gln50-mutated BLUF domains of the PixD protein of Thermosynechococcus elongatus BP-1: photoconversion at low temperature without Tyr8.
    Biochemistry, 2008, Jan-15, Volume: 47, Issue:2

    Topics: Absorption; Anions; Bacterial Proteins; Cyanobacteria; Flavin-Adenine Dinucleotide; Glutamine; Hydrogen Bonding; Light; Mutant Proteins; Protein Structure, Tertiary; Temperature; Time Factors; Tyrosine

2008
Peroxynitrite-mediated oxidative modifications of complex II: relevance in myocardial infarction.
    Biochemistry, 2010, Mar-23, Volume: 49, Issue:11

    Topics: Amino Acid Sequence; Animals; Cell Hypoxia; Cyclic N-Oxides; Cysteine; Disulfides; Electron Transport Complex II; Flavin-Adenine Dinucleotide; Humans; Molecular Sequence Data; Molecular Weight; Muscle Cells; Myocardial Infarction; Oxidation-Reduction; Peroxynitrous Acid; Protein Subunits; Rats; Rats, Sprague-Dawley; Tyrosine

2010
A temperature-dependent conformational change of NADH oxidase from Thermus thermophilus HB8.
    Proteins, 2012, Volume: 80, Issue:2

    Topics: Binding Sites; Catalytic Domain; Circular Dichroism; Flavin-Adenine Dinucleotide; Light; Models, Molecular; Molecular Dynamics Simulation; Multienzyme Complexes; Mutagenesis, Site-Directed; NADH, NADPH Oxidoreductases; Protein Conformation; Scattering, Radiation; Spectrometry, Fluorescence; Temperature; Thermus thermophilus; Tryptophan; Tyrosine

2012
On the autofluorescence of fingermarks.
    Forensic science international, 2012, Oct-10, Volume: 222, Issue:1-3

    Topics: beta Carotene; Bilirubin; Chlorophyll; Chromatography, Thin Layer; Dermatoglyphics; Flavin-Adenine Dinucleotide; Fluorescence; Humans; Kynurenine; Light; Phenylalanine; Pheophytins; Protoporphyrins; Riboflavin; Sebum; Spectrometry, Fluorescence; Sweat; Thiamine; Tryptophan; Tyrosine; Ultraviolet Rays; Vitamin B 6; Xanthurenates

2012
Structure and function of ∆1-tetrahydrocannabinolic acid (THCA) synthase, the enzyme controlling the psychoactivity of Cannabis sativa.
    Journal of molecular biology, 2012, Oct-12, Volume: 423, Issue:1

    Topics: Animals; Berberine; Cannabis; Carbon Dioxide; Crystallography, X-Ray; Cysteine; Flavin-Adenine Dinucleotide; Glutamic Acid; Histidine; Intramolecular Oxidoreductases; Mutation; Protein Structure, Tertiary; Psychotropic Drugs; Structure-Activity Relationship; Tyrosine

2012
Variable electron transfer pathways in an amphibian cryptochrome: tryptophan versus tyrosine-based radical pairs.
    The Journal of biological chemistry, 2013, Mar-29, Volume: 288, Issue:13

    Topics: Amphibians; Animals; Cryptochromes; Deoxyribodipyrimidine Photo-Lyase; Electron Spin Resonance Spectroscopy; Electron Transport; Flavin-Adenine Dinucleotide; Kinetics; Light; Models, Molecular; Molecular Conformation; Optics and Photonics; Photochemistry; Spectrophotometry, Ultraviolet; Tryptophan; Tyrosine

2013
Charge transfer in E. coli DNA photolyase: understanding polarization and stabilization effects via QM/MM simulations.
    The journal of physical chemistry. B, 2013, Sep-19, Volume: 117, Issue:37

    Topics: Deoxyribodipyrimidine Photo-Lyase; Electron Transport; Enzyme Stability; Escherichia coli Proteins; Flavin-Adenine Dinucleotide; Kinetics; Models, Molecular; Molecular Dynamics Simulation; Protein Conformation; Static Electricity; Tryptophan; Tyrosine

2013
Fluorescence spectral diagnosis of malaria: a preliminary study.
    Diagnostic pathology, 2014, Oct-17, Volume: 9

    Topics: Adolescent; Biomarkers; Case-Control Studies; Child; Female; Flavin-Adenine Dinucleotide; Humans; Malaria; Male; NAD; Porphyrins; Sensitivity and Specificity; Spectrometry, Fluorescence; Tryptophan; Tyrosine; Young Adult

2014
Replacement of Tyr50 stacked on the si-face of the isoalloxazine ring of the flavin adenine dinucleotide prosthetic group modulates Bacillus subtilis ferredoxin-NADP(+) oxidoreductase activity toward NADPH.
    Photosynthesis research, 2015, Volume: 125, Issue:1-2

    Topics: Amino Acid Sequence; Bacillus subtilis; Bacterial Proteins; Ferredoxin-NADP Reductase; Ferredoxins; Flavin-Adenine Dinucleotide; Flavins; Models, Molecular; Molecular Sequence Data; Mutation, Missense; NADP; Sequence Alignment; Tyrosine

2015
Flavin-Protein Complexes: Aromatic Stacking Assisted by a Hydrogen Bond.
    Biochemistry, 2015, Jul-21, Volume: 54, Issue:28

    Topics: Amino Acid Sequence; Bacillus subtilis; Catalytic Domain; Flavin-Adenine Dinucleotide; Flavins; Hydrogen Bonding; Methylation; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Protein Conformation; tRNA Methyltransferases; Tyrosine

2015
New insights into xanthine oxidase behavior upon heating using spectroscopy and in silico approach.
    International journal of biological macromolecules, 2016, Volume: 88

    Topics: Animals; Cattle; Circular Dichroism; Dinitrocresols; Flavin-Adenine Dinucleotide; Hot Temperature; Milk; Molecular Dynamics Simulation; Protein Conformation; Protein Multimerization; Protein Subunits; Spectrometry, Fluorescence; Tryptophan; Tyrosine; Xanthine Oxidase

2016
Photoactivation of the BLUF Protein PixD Probed by the Site-Specific Incorporation of Fluorotyrosine Residues.
    Journal of the American Chemical Society, 2017, 10-18, Volume: 139, Issue:41

    Topics: Bacterial Proteins; Binding Sites; Color; Electron Transport; Flavin-Adenine Dinucleotide; Flavoproteins; Fluorine; Hydrogen Bonding; Hydrogen-Ion Concentration; Light; Photoreceptors, Microbial; Protein Domains; Protons; Synechocystis; Tyrosine

2017
Tyrosine Residues 232 and 401 Play a Critical Role in the Binding of the Cofactor FAD of Acyl-coA Oxidase.
    Applied biochemistry and biotechnology, 2018, Volume: 185, Issue:4

    Topics: Acyl-CoA Oxidase; Escherichia coli; Escherichia coli Proteins; Flavin-Adenine Dinucleotide; Protein Binding; Tyrosine

2018
Ultrafast photoinduced flavin dynamics in the unusual active site of the tRNA methyltransferase TrmFO.
    Physical chemistry chemical physics : PCCP, 2019, Apr-24, Volume: 21, Issue:17

    Topics: Adenine; Amino Acid Sequence; Bacillus subtilis; Binding Sites; Cysteine; Flavin-Adenine Dinucleotide; Flavins; Kinetics; Models, Molecular; Oxidation-Reduction; Photochemical Processes; Protein Binding; tRNA Methyltransferases; Tyrosine

2019
Short-Lived Radical Intermediates in the Photochemistry of Glucose Oxidase.
    Chemphyschem : a European journal of chemical physics and physical chemistry, 2019, 07-16, Volume: 20, Issue:14

    Topics: Aspergillus niger; Flavin-Adenine Dinucleotide; Free Radicals; Fungal Proteins; Glucose Oxidase; Kinetics; Light; Photochemistry; Spectrometry, Fluorescence; Tyrosine

2019
Rapid Oxidation Following Photoreduction in the Avian Cryptochrome4 Photocycle.
    Biochemistry, 2020, 09-29, Volume: 59, Issue:38

    Topics: Animals; Avian Proteins; Chickens; Cryptochromes; Dithiothreitol; Flavin-Adenine Dinucleotide; Free Radicals; Light; Oxidation-Reduction; Photolysis; Tyrosine

2020
Spectroscopic and Computational Observation of Glutamine Tautomerization in the Blue Light Sensing Using Flavin Domain Photoreaction.
    Journal of the American Chemical Society, 2023, 01-18, Volume: 145, Issue:2

    Topics: Bacterial Proteins; Flavin-Adenine Dinucleotide; Glutamine; Light; Organic Chemicals; Photoreceptors, Microbial; Protons; Spectroscopy, Fourier Transform Infrared; Tyrosine

2023