tryptophan and tryptophan tryptophylquinone

tryptophan has been researched along with tryptophan tryptophylquinone in 101 studies

Research

Studies (101)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	41 (40.59)	18.2507
2000's	31 (30.69)	29.6817
2010's	28 (27.72)	24.3611
2020's	1 (0.99)	2.80

Authors

Authors	Studies
Duine, JA	3
Duine, JA; Hol, WG; Huitema, F; Huizinga, EG; Jongejan, JA; van Zanten, BA; Wilson, KS	1
Davidson, VL; Graichen, ME; Jones, LH	2
Chen, LY; Davidson, VL; Duine, JA; Hol, WG; Huizinga, EG; Mathews, FS; Vellieux, FM	1
Bishop, GR; Davidson, VL	2
Davidson, VL; Hyun, YL	2
Davidson, VL; Jones, LH	1
de Vries, S; Duine, JA; Gorren, AC	1
Davidson, VL; Edwards, SL; Hyun, YL; Wingfield, PT	1
Kuusk, V; McIntire, WS	1
Klinman, JP; Mu, D	1
Chen, L; Davidson, VL; Durley, RC; Mathews, FS	1
McIntire, WS	2
Chistoserdov, AY; Davidson, VL; Edwards, SL; Eisenstein, E; Govindaraj, S; Jones, LH; Sanders-Loehr, J	1
Ferguson, SJ; Page, MD	1
Brooks, HB; Davidson, VL; Jones, LH	1
Itoh, S; Ohshiro, Y	1
Brooks, HB; Davidson, VL; Graichen, ME; Hyun, YL; Jones, LH	1
Mathews, FS	1
Lidstrom, ME	1
Tanizawa, K	2
Brodersen, DE; Chen, Z; Davidson, VL; Durley, RC; Mathews, FS; Merli, A; Morini, B; Rossi, GL	1
Duine, JA; Fukuzumi, S; Gorren, AC; Itoh, S; Moënne-Loccoz, P; Nakamura, N; Sanders-Loehr, J	1
Bishop, GR; Brooks, HB; Davidson, VL	1
Anthony, C	1
Hartmann, C; McIntire, WS	1
Davidson, VL; Graichen, ME; Hosler, JP; Jones, LH; Mathews, FS	1
Davidson, VL; Zhu, Z	2
Chen, ZW; Ferrari, D; Kuusk, V; Labesse, G; Mathews, FS; McIntire, WS; Rossi, GL	1
Basran, J; Scrutton, NS; Sutcliffe, MJ	1
Davidson, VL	6
Davidson, VL; Hyun, YL; Zhu, Z	1
Ikeda, T; Kano, K; Sato, A; Takagi, K; Torimura, M	1
Mitchell, AE; Rucker, RB; Stites, TE	1
Basran, J; Patel, S; Scrutton, NS; Sutcliffe, MJ	1
Klinman, JP; Schwartz, B	1
Adachi, O; Devreese, B; Duine, JA; Hacisalihoglu, A; Iwabuki, H; Jongejan, JA; Kim, JK; Kuroda, S; Okajima, T; Tanizawa, K; Van Beeumen, J; Vandenberghe, I	1
Davidson, VL; Jones, LH; Mathews, FS; Sun, D	1
Fukuzumi, S; Itoh, S	1
Davidson, VL; Sun, D	2
Carbonera, D; Di Valentin, M; Ferrari, D; Merli, A; Peracchi, A; Rossi, GL	1
Liang, JM; Yu, CH; Zou, JW	1
Davidson, VL; Graichen, ME; Liu, A; Pearson, AR; Wang, Y; Wilmot, CM	1
Agger, SA; Davidson, VL; De La Mora-Rey, T; Graichen, ME; Grimsrud, PA; Jones, LH; Marimanikkupam, S; Pearson, AR; Wang, Y; Wilmot, CM	1
Davidson, VL; Jones, LH; Pearson, AR; Tang, Y; Wilmot, CM	1
Klinman, JP; Limburg, J; Mure, M	1
Davidson, VL; Jones, LH; Li, X; Pearson, AR; Wang, Y; Wilmot, CM	1
Combe, JP; Hothi, P; Khadra, KA; Leys, D; Scrutton, NS	1
Davidson, VL; Feng, M; Li, X; Tachikawa, H; Wang, Y	1
Davidson, VL; Li, X; Marimanikkuppam, S; Pearson, AR; Wilmot, CM	1
Davidson, VL; Jones, LH; Li, X; Pearson, AR; Wilmot, CM	1
Bellamy, HD; Chen, ZW; Chistoserdov, A; Davidson, VL; Ferrari, D; Mathews, FS; Merli, A; Rossi, GL; Sukumar, N	1
Fujieda, N; Fukuzumi, S; Hasegawa, T; Itoh, S; Kano, K; Murakami, Y; Ohkubo, K; Yoshimoto, N	1
Cullis, PM; Hothi, P; Lee, M; Leys, D; Scrutton, NS	1
Davidson, VL; Fu, R; Li, X; Liu, A	1
Biermann, N; Cavalieri, C; Einsle, O; Ferrari, D; Merli, A; Rossi, GL; Ubbink, M; Vlasie, MD	1
Davidson, VL; Fu, R; Krebs, C; Lee, S; Li, X; Liu, A	1
Davidson, VL; Lee, S; Li, X; Shin, S	1
Davidson, VL; Wilmot, CM	2
de Visser, SP; Pang, J; Scrutton, NS; Sutcliffe, MJ	1
Bollinger, JM; Matthews, ML	1
Davidson, VL; Jensen, LM; Sanishvili, R; Wilmot, CM	1
Abu Tarboush, N; Davidson, VL; Shin, S	1
Chen, Y; Davidson, VL; Feng, M; Jensen, LM; Liu, A; Shin, S; Tachikawa, H; Wilmot, CM	1
Davidson, VL; Goblirsch, BR; Wilmot, CM; Yukl, ET	1
Nakai, T; Okajima, T; Tanizawa, K	1
Davidson, VL; Geng, J; Jensen, LM; Liu, A; Tarboush, NA; Wilmot, CM; Yukl, ET	1
Davidson, VL; Feng, M; Jensen, LM; Liu, A; Wei, X; Wilmot, CM; Yukl, ET	1
Davidson, VL; Liu, A	1
Wilmot, CM; Yukl, ET	2
Abu Tarboush, N; Davidson, VL; Geng, J; Liu, A; Shin, S	1
Davidson, VL; Jensen, LM; Krzystek, J; Liu, A; Liu, F; Shin, S; Wilmot, CM; Yukl, ET	1
Abu Tarboush, N; Davidson, VL; Jensen, LM; Wilmot, CM	1
Davidson, VL; Dornevil, K; Geng, J; Liu, A	1
Davidson, VL; Jensen, LM; Wilmot, CM; Yukl, ET	1
Abu Tarboush, N; Davidson, VL; Feng, M; Shin, S; Wilmot, CM; Yukl, ET	1
Davidson, VL; Feng, M; Shin, S	1
Davidson, VL; Shin, S	1
Bonnot, F; Klinman, JP	1
Davis, I; Geng, J; Liu, A; Liu, F	1
Davis, I; Geng, J; Liu, A	1
Choi, M; Davidson, VL; Feng, M; Li, C; Shin, S; Williamson, HR; Wilmot, CM	1
Davidson, VL; Ma, Z	1
Davidson, VL; Yukl, ET	1
Barik, S	1

Reviews

25 review(s) available for tryptophan and tryptophan tryptophylquinone

Article	Year
Quinoproteins: enzymes containing the quinonoid cofactor pyrroloquinoline quinone, topaquinone or tryptophan-tryptophan quinone. European journal of biochemistry, 1991, Sep-01, Volume: 200, Issue:2 Topics: Coenzymes; Dihydroxyphenylalanine; Enzymes; Gram-Negative Bacteria; Indolequinones; Molecular Conformation; Oxidoreductases; PQQ Cofactor; Protein Conformation; Quinolones; Quinones; Tryptophan	1991
Quinoenzymes in biology. Annual review of biochemistry, 1994, Volume: 63 Topics: Amino Acid Sequence; Animals; Coenzymes; Dihydroxyphenylalanine; Indolequinones; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; PQQ Cofactor; Quinolones; Quinones; Sequence Homology, Amino Acid; Tryptophan	1994
Quinoproteins. FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 1994, Volume: 8, Issue:8 Topics: Coenzymes; Dihydroxyphenylalanine; Indolequinones; Oxidation-Reduction; PQQ Cofactor; Quinolones; Quinones; Tryptophan	1994
Biogenesis of novel quinone coenzymes. Journal of biochemistry, 1995, Volume: 118, Issue:4 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Animals; Coenzymes; Dihydroxyphenylalanine; Humans; Indolequinones; Molecular Sequence Data; Oxidoreductases Acting on CH-NH Group Donors; Quinones; Sequence Alignment; Tryptophan	1995
Quinoprotein-catalysed reactions. The Biochemical journal, 1996, Dec-15, Volume: 320 ( Pt 3) Topics: Alcohol Oxidoreductases; Amine Oxidase (Copper-Containing); Bacterial Proteins; Binding Sites; Coenzymes; Dihydroxyphenylalanine; Disulfides; Electron Transport; Indolequinones; Lysine; Models, Chemical; Models, Molecular; Molecular Structure; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; PQQ Cofactor; Protein-Lysine 6-Oxidase; Quinolones; Quinones; Tryptophan	1996
Methylamine dehydrogenase: structure and function of electron transfer complexes. Biochemical Society transactions, 1999, Volume: 27, Issue:2 Topics: Bacterial Proteins; Copper; Cytochrome c Group; Electron Transport; Indolequinones; Kinetics; Models, Chemical; Models, Molecular; Multienzyme Complexes; Mutation; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Quinones; Tryptophan	1999
[Built-in cofactors: amino acid residue-derived new cofactors]. Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, 1999, Volume: 44, Issue:13 Topics: Amino Acids; Animals; Catalysis; Coenzymes; Dihydroxyphenylalanine; Indolequinones; Lysine; Protein Processing, Post-Translational; Quinones; Tryptophan	1999
Physiological importance of quinoenzymes and the O-quinone family of cofactors. The Journal of nutrition, 2000, Volume: 130, Issue:4 Topics: Animals; Coenzymes; Dihydroxyphenylalanine; Enzymes; Humans; Indolequinones; Lysine; PQQ Cofactor; Quinolones; Quinones; Tryptophan	2000
Mechanisms of biosynthesis of protein-derived redox cofactors. Vitamins and hormones, 2001, Volume: 61 Topics: Amino Acid Oxidoreductases; Amino Acids; Coenzymes; Dihydroxyphenylalanine; Galactose Oxidase; Indolequinones; Lysine; Oxidation-Reduction; Quinones; Tryptophan	2001
Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase. Advances in protein chemistry, 2001, Volume: 58 Topics: Alcohol Oxidoreductases; Indolequinones; Oxidoreductases Acting on CH-NH Group Donors; PQQ Cofactor; Quinolones; Quinones; Tryptophan	2001
Catalytic control of redox reactivities of coenzyme analogs by metal ions. Antioxidants & redox signaling, 2001, Volume: 3, Issue:5 Topics: Catalysis; Flavins; Hydrogen; Indolequinones; Ions; Models, Chemical; Models, Molecular; Oxidation-Reduction; Quinones; Superoxide Dismutase; Tryptophan	2001
Electron transfer in quinoproteins. Archives of biochemistry and biophysics, 2004, Aug-01, Volume: 428, Issue:1 Topics: Binding Sites; Electron Transport; Enzyme Activation; Indolequinones; Models, Chemical; Models, Molecular; Oxidoreductases; PQQ Cofactor; Protein Binding; Protein Conformation; Structure-Activity Relationship; Tryptophan	2004
Structure and mechanism of tryptophylquinone enzymes. Bioorganic chemistry, 2005, Volume: 33, Issue:3 Topics: Catalysis; Crystallography, X-Ray; Electron Transport; Indolequinones; Models, Molecular; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Protein Conformation; Protein Structure, Secondary; Tryptophan	2005
Uncovering novel biochemistry in the mechanism of tryptophan tryptophylquinone cofactor biosynthesis. Current opinion in chemical biology, 2009, Volume: 13, Issue:4 Topics: Coenzymes; Indolequinones; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Tryptophan	2009
[Mechanisms of biosynthesis of built-in cofactors]. Seikagaku. The Journal of Japanese Biochemical Society, 2011, Volume: 83, Issue:8 Topics: Amine Oxidase (Copper-Containing); Amino Acid Sequence; Animals; Catalysis; Codon, Terminator; Coenzymes; Copper; Crystallography, X-Ray; Dihydroxyphenylalanine; Dipeptides; Endonucleases; Humans; Indolequinones; Ions; Molecular Sequence Data; Oxidoreductases Acting on CH-NH Group Donors; RNA-Directed DNA Polymerase; Tryptophan	2011
Tryptophan tryptophylquinone biosynthesis: a radical approach to posttranslational modification. Biochimica et biophysica acta, 2012, Volume: 1824, Issue:11 Topics: Bacterial Proteins; Biocatalysis; Coenzymes; Free Radicals; Heme; Indolequinones; Iron-Sulfur Proteins; Models, Molecular; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Processing, Post-Translational; Tryptophan	2012
Cofactor biosynthesis through protein post-translational modification. Current opinion in chemical biology, 2012, Volume: 16, Issue:1-2 Topics: Amino Acids; Humans; Indolequinones; Ligands; Metals; Protein Processing, Post-Translational; Tryptophan	2012
MauG: a di-heme enzyme required for methylamine dehydrogenase maturation. Dalton transactions (Cambridge, England : 2003), 2013, Mar-07, Volume: 42, Issue:9 Topics: Crystallography, X-Ray; Electron Transport; Endopeptidases; Heme; Indolequinones; Oxidoreductases Acting on CH-NH Group Donors; Tryptophan	2013
Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone. Annual review of biochemistry, 2013, Volume: 82 Topics: Catalysis; Electron Transport; Heme; Indolequinones; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Processing, Post-Translational; Tryptophan	2013
MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis. Archives of biochemistry and biophysics, 2014, Feb-15, Volume: 544 Topics: Bacteria; Electron Transport; Heme; Heme Oxygenase (Decyclizing); Indolequinones; Models, Molecular; Peroxidase; Tryptophan	2014
Intrigues and intricacies of the biosynthetic pathways for the enzymatic quinocofactors: PQQ, TTQ, CTQ, TPQ, and LTQ. Chemical reviews, 2014, Apr-23, Volume: 114, Issue:8 Topics: Animals; Coenzymes; Dihydroxyphenylalanine; Dipeptides; Humans; Indolequinones; Lysine; PQQ Cofactor; Quinones; Tryptophan	2014
Bis-Fe(IV): nature's sniper for long-range oxidation. Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2014, Volume: 19, Issue:7 Topics: Indolequinones; Iron Compounds; Models, Molecular; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus; Tryptophan	2014
Protein-Derived Cofactors Revisited: Empowering Amino Acid Residues with New Functions. Biochemistry, 2018, 06-05, Volume: 57, Issue:22 Topics: Amino Acids; Coenzymes; Dipeptides; Electron Transport; Heme; Humans; Indolequinones; Lysine; Models, Molecular; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Protein Processing, Post-Translational; Quinones; Tryptophan	2018
Diversity of structures, catalytic mechanisms and processes of cofactor biosynthesis of tryptophylquinone-bearing enzymes. Archives of biochemistry and biophysics, 2018, 09-15, Volume: 654 Topics: Catalysis; Coenzymes; Indolequinones; Protein Conformation; Protein Processing, Post-Translational; Tryptophan	2018
The Uniqueness of Tryptophan in Biology: Properties, Metabolism, Interactions and Localization in Proteins. International journal of molecular sciences, 2020, Nov-20, Volume: 21, Issue:22 Topics: Animals; Codon; Dipeptides; Humans; Hydrophobic and Hydrophilic Interactions; Indolequinones; Indoles; Kynurenine; Protein Biosynthesis; Protein Interaction Domains and Motifs; Proteins; Serotonin; Structure-Activity Relationship; Thermodynamics; Tryptophan	2020

Other Studies

76 other study(ies) available for tryptophan and tryptophan tryptophylquinone

Article	Year
The quinoid cofactors, pyrroloquinoline quinone (PQQ), topaquinone (TPQ) and tryptophan tryptophylquinone (TTQ). Journal of nutritional science and vitaminology, 1992, Volume: Spec No Topics: Animals; Coenzymes; Dihydroxyphenylalanine; Humans; Indolequinones; Molecular Structure; PQQ Cofactor; Quinolones; Quinones; Tryptophan	1992
Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor. Biochemistry, 1992, Oct-13, Volume: 31, Issue:40 Topics: Amino Acid Sequence; Binding Sites; Hydrazines; Indolequinones; Molecular Sequence Data; Oxidoreductases Acting on CH-NH Group Donors; Protein Conformation; Quinones; Thiobacillus; Tryptophan	1992
Reactions of benzylamines with methylamine dehydrogenase. Evidence for a carbanionic reaction intermediate and reaction mechanism similar to eukaryotic quinoproteins. Biochemistry, 1992, Apr-07, Volume: 31, Issue:13 Topics: Anions; Bacterial Proteins; Benzylamines; Binding, Competitive; Electron Transport; Indolequinones; Kinetics; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Phenazines; Quinones; Spectrophotometry; Tryptophan	1992
Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase. FEBS letters, 1991, Aug-05, Volume: 287, Issue:1-2 Topics: Binding Sites; Hydrogen Bonding; Indolequinones; Macromolecular Substances; Models, Molecular; Molecular Structure; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Quinones; Thiobacillus; Tryptophan; X-Ray Diffraction	1991
Intermolecular electron transfer from substrate-reduced methylamine dehydrogenase to amicyanin is linked to proton transfer. Biochemistry, 1995, Sep-19, Volume: 34, Issue:37 Topics: Bacterial Proteins; Copper; Electron Transport; Indolequinones; Kinetics; Molecular Structure; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protons; Quinones; Substrate Specificity; Thermodynamics; Tryptophan	1995
Electron transfer reactions between aromatic amine dehydrogenase and azurin. Biochemistry, 1995, Sep-26, Volume: 34, Issue:38 Topics: Alcaligenes; Azurin; Bacterial Proteins; Dithionite; Electron Transport; Flow Injection Analysis; Indolequinones; Kinetics; Models, Chemical; Oxidoreductases Acting on CH-NH Group Donors; Protein Binding; Quinones; Spectrophotometry; Substrate Specificity; Tryptophan; Tyramine	1995
Reaction mechanism for the inactivation of the quinoprotein methylamine dehydrogenase by phenylhydrazine. Biochimica et biophysica acta, 1995, Sep-27, Volume: 1252, Issue:1 Topics: Indolequinones; Kinetics; Oxidoreductases Acting on CH-NH Group Donors; Phenylhydrazines; Quinones; Structure-Activity Relationship; Tryptophan	1995
Binding of monovalent cations to methylamine dehydrogenase in the semiquinone state and its effect on electron transfer. Biochemistry, 1995, Aug-01, Volume: 34, Issue:30 Topics: Bacterial Proteins; Binding Sites; Cations, Monovalent; Cesium; Electron Spin Resonance Spectroscopy; Electron Transport; Hydrogen-Ion Concentration; Indolequinones; Kinetics; Light; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Quaternary Ammonium Compounds; Quinones; Sodium; Spectrophotometry; Tryptophan	1995
Mechanism of reaction of allylamine with the quinoprotein methylamine dehydrogenase. The Biochemical journal, 1995, Jun-01, Volume: 308 ( Pt 2) Topics: Allylamine; Bacterial Proteins; Indolequinones; Kinetics; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Quinones; Tryptophan	1995
Mechanistic studies of aromatic amine dehydrogenase, a tryptophan tryptophylquinone enzyme. Biochemistry, 1995, Jan-24, Volume: 34, Issue:3 Topics: Alcaligenes; Benzylamines; Indolequinones; Kinetics; Mutagenesis, Site-Directed; Oxidoreductases Acting on CH-NH Group Donors; Phenethylamines; Quinones; Spectrum Analysis; Structure-Activity Relationship; Tryptophan	1995
Spectroscopic evidence for a common electron transfer pathway for two tryptophan tryptophylquinone enzymes. The Journal of biological chemistry, 1995, Mar-03, Volume: 270, Issue:9 Topics: Alcaligenes; Azurin; Circular Dichroism; Cytochrome c Group; Electron Transport; Indolequinones; Oxidoreductases Acting on CH-NH Group Donors; Quinones; Spectrophotometry, Ultraviolet; Tryptophan	1995
Influence of monovalent cations on the ultraviolet-visible spectrum of tryptophan tryptophylquinone-containing methylamine dehydrogenase from bacterium W3A1. The Journal of biological chemistry, 1994, Oct-21, Volume: 269, Issue:42 Topics: Bacteria; Binding Sites; Hydrogen-Ion Concentration; Indolequinones; Lithium; Oxidoreductases Acting on CH-NH Group Donors; Potassium; Quinones; Sodium; Spectrophotometry, Ultraviolet; Tryptophan	1994
Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i. Science (New York, N.Y.), 1994, Apr-01, Volume: 264, Issue:5155 Topics: Bacterial Proteins; Computer Graphics; Cytochrome c Group; Electron Transport; Hydrogen Bonding; Indolequinones; Models, Molecular; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Conformation; Protein Folding; Protein Structure, Secondary; Quinones; Software; Tryptophan	1994
Aromatic amine dehydrogenase, a second tryptophan tryptophylquinone enzyme. Journal of bacteriology, 1994, Volume: 176, Issue:10 Topics: Alcaligenes; Amino Acid Sequence; Antibodies, Bacterial; Cross Reactions; Indolequinones; Molecular Sequence Data; Molecular Weight; Nucleic Acid Hybridization; Oxidoreductases Acting on CH-NH Group Donors; Quinones; Sequence Analysis; Spectrophotometry; Spectrum Analysis, Raman; Tryptophan	1994
Mutants of Methylobacterium extorquens and Paracoccus denitrificans deficient in c-type cytochrome biogenesis synthesise the methylamine-dehydrogenase polypeptides but cannot assemble the tryptophan-tryptophylquinone group. European journal of biochemistry, 1993, Dec-01, Volume: 218, Issue:2 Topics: Benzoquinones; Choline; Cytochrome c Group; Gram-Negative Aerobic Bacteria; Indolequinones; Methylamines; Mutation; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Peptides; Quinones; Tryptophan	1993
Deuterium kinetic isotope effect and stopped-flow kinetic studies of the quinoprotein methylamine dehydrogenase. Biochemistry, 1993, Mar-16, Volume: 32, Issue:10 Topics: Deuterium; Indolequinones; Isotope Labeling; Kinetics; Mathematics; Models, Theoretical; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Quinones; Substrate Specificity; Tryptophan	1993
Tryptophan tryptophylquinone in bacterial amine dehydrogenases. Methods in enzymology, 1995, Volume: 258 Topics: Amino Acid Sequence; Amino Acids; Bacteria; Chromatography, High Pressure Liquid; Chromatography, Ion Exchange; Endopeptidases; Indicators and Reagents; Indolequinones; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Peptide Fragments; Pronase; Quinones; Spectrometry, Mass, Fast Atom Bombardment; Spectrophotometry; Tryptophan	1995
Model studies of cofactor tryptophan tryptophylquinone. Methods in enzymology, 1995, Volume: 258 Topics: Indicators and Reagents; Indolequinones; Magnetic Resonance Spectroscopy; Mass Spectrometry; Models, Chemical; Models, Molecular; Molecular Conformation; Molecular Structure; Quinones; Spectrophotometry, Infrared; Structure-Activity Relationship; Tryptophan	1995
Detection of intermediates in tryptophan tryptophylquinone enzymes. Methods in enzymology, 1995, Volume: 258 Topics: Alcaligenes; Ammonia; Bacteria; Dithionite; Indolequinones; Kinetics; Molecular Structure; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Quinones; Spectrophotometry; Tryptophan	1995
X-ray studies of quinoproteins. Methods in enzymology, 1995, Volume: 258 Topics: Alcohol Oxidoreductases; Amino Acid Sequence; Binding Sites; Crystallization; Crystallography, X-Ray; Euryarchaeota; Galactose Oxidase; Indolequinones; Macromolecular Substances; Models, Molecular; Molecular Sequence Data; Neuraminidase; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; PQQ Cofactor; Protein Conformation; Protein Folding; Protein Structure, Secondary; Quinolones; Quinones; Thiobacillus; Tryptophan	1995
Genetics of bacterial quinoproteins. Methods in enzymology, 1995, Volume: 258 Topics: Alcohol Dehydrogenase; Alcohol Oxidoreductases; Bacteria; Bacterial Proteins; Cloning, Molecular; Gene Expression; Genes, Bacterial; Genetic Complementation Test; Glucose 1-Dehydrogenase; Glucose Dehydrogenases; Indolequinones; Mutagenesis; Oligonucleotide Probes; Oxidoreductases Acting on CH-NH Group Donors; PQQ Cofactor; Quinolones; Quinones; Recombinant Proteins; Species Specificity; Tryptophan	1995
Enzymatic and electron transfer activities in crystalline protein complexes. The Journal of biological chemistry, 1996, Apr-19, Volume: 271, Issue:16 Topics: Bacterial Proteins; Binding Sites; Copper; Crystallization; Cytochrome c Group; Electron Transport; Heme; Indolequinones; Macromolecular Substances; Models, Structural; Oxidoreductases Acting on CH-NH Group Donors; Protein Structure, Secondary; Quinones; Spectrophotometry; Tryptophan	1996
Electrostatic environment of the tryptophylquinone cofactor in methylamine dehydrogenase: evidence from resonance Raman spectroscopy of model compounds. Biochemistry, 1996, Apr-16, Volume: 35, Issue:15 Topics: Catalysis; Hydrogen Bonding; Indolequinones; Indoles; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Quinones; Spectrum Analysis, Raman; Tryptophan	1996
Evidence for a tryptophan tryptophylquinone aminosemiquinone intermediate in the physiologic reaction between methylamine dehydrogenase and amicyanin. Biochemistry, 1996, Jul-09, Volume: 35, Issue:27 Topics: Ammonium Chloride; Bacterial Proteins; Free Radicals; Indolequinones; Kinetics; Models, Chemical; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Quinones; Spectrophotometry; Tryptophan	1996
Tryptophan-derived cofactors functioning in oxidoreductases. Advances in experimental medicine and biology, 1996, Volume: 398 Topics: Coenzymes; Dihydroxyphenylalanine; Indolequinones; Molecular Structure; Oxidoreductases; Paracoccus denitrificans; PQQ Cofactor; Quinolones; Quinones; Tryptophan	1996
Amine-oxidizing quinoproteins. Methods in enzymology, 1997, Volume: 280 Topics: Amino Acid Sequence; Coenzymes; Copper; Diabetes Mellitus; Dihydroxyphenylalanine; Electron Spin Resonance Spectroscopy; Enzyme Inhibitors; Heart Failure; Humans; Indolequinones; Liver Cirrhosis; Lysine; Menkes Kinky Hair Syndrome; Metalloproteins; Mixed Function Oxygenases; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; PQQ Cofactor; Protein-Lysine 6-Oxidase; Quinolones; Quinones; Semicarbazides; Sequence Homology, Amino Acid; Spectrum Analysis, Raman; Stereoisomerism; Substrate Specificity; Tryptophan	1997
Factors which stabilize the methylamine dehydrogenase-amicyanin electron transfer protein complex revealed by site-directed mutagenesis. Biochemistry, 1997, Oct-21, Volume: 36, Issue:42 Topics: Amino Acid Sequence; Amino Acid Substitution; Arginine; Bacterial Proteins; Cloning, Molecular; Copper; Escherichia coli; Glutamic Acid; Indolequinones; Lysine; Metalloproteins; Models, Molecular; Mutagenesis, Site-Directed; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Phenylalanine; Protein Conformation; Quinones; Recombinant Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Tryptophan	1997
Kinetic and chemical mechanisms for the effects of univalent cations on the spectral properties of aromatic amine dehydrogenase. The Biochemical journal, 1998, Jan-01, Volume: 329 ( Pt 1) Topics: Alcaligenes; Ammonia; Cations, Monovalent; Hydrogen-Ion Concentration; Indolequinones; Kinetics; Metals, Alkali; Molecular Structure; Oxidoreductases Acting on CH-NH Group Donors; Potassium; Protein Binding; Quinones; Sodium; Spectrophotometry; Tryptophan	1998
Redox properties of tryptophan tryptophylquinone enzymes. Correlation with structure and reactivity. The Journal of biological chemistry, 1998, Jun-05, Volume: 273, Issue:23 Topics: Benzoquinones; Binding Sites; Electrochemistry; Electron Transport; Hydrogen-Ion Concentration; Indolequinones; Models, Molecular; Molecular Structure; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protons; Quinones; Spectrophotometry; Structure-Activity Relationship; Tryptophan	1998
Electron transfer from the aminosemiquinone reaction intermediate of methylamine dehydrogenase to amicyanin. Biochemistry, 1998, Aug-04, Volume: 37, Issue:31 Topics: Bacterial Proteins; Electron Transport; Hydrogen-Ion Concentration; Indolequinones; Kinetics; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Potassium Chloride; Protons; Quinones; Solvents; Tryptophan	1998
Crystallographic and spectroscopic studies of native, aminoquinol, and monovalent cation-bound forms of methylamine dehydrogenase from Methylobacterium extorquens AM1. The Journal of biological chemistry, 1998, Oct-02, Volume: 273, Issue:40 Topics: Bacterial Proteins; Binding Sites; Cesium; Crystallography, X-Ray; Indolequinones; Methylamines; Models, Molecular; Oxidoreductases Acting on CH-NH Group Donors; Quinones; Spectrophotometry; Tryptophan	1998
Enzymatic H-transfer requires vibration-driven extreme tunneling. Biochemistry, 1999, Mar-09, Volume: 38, Issue:10 Topics: Hydrogen Bonding; Indolequinones; Kinetics; Methanococcaceae; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Quinones; Spectrophotometry; Substrate Specificity; Temperature; Thermodynamics; Tryptophan	1999
Gated and ungated electron transfer reactions from aromatic amine dehydrogenase to azurin. The Journal of biological chemistry, 1999, Oct-08, Volume: 274, Issue:41 Topics: Alcaligenes; Azurin; Benzoquinones; Dithionite; Electron Transport; Indolequinones; Kinetics; Molecular Structure; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Quinones; Thermodynamics; Tryptophan	1999
Protein redox potential measurements based on kinetic analysis with mediated continuous-flow column electrolytic spectroelectrochemical technique. Application to TTQ-containing methylamine dehydrogenase. Analytical chemistry, 2000, Jan-01, Volume: 72, Issue:1 Topics: Electrochemistry; Indolequinones; Kinetics; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Quinones; Spectrophotometry; Tryptophan	2000
Structure, function, and applications of tryptophan tryptophylquinone enzymes. Advances in experimental medicine and biology, 1999, Volume: 467 Topics: Bacterial Proteins; Biosensing Techniques; Electron Transport; Indolequinones; Models, Molecular; Mutagenesis, Site-Directed; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Quinones; Recombinant Proteins; Tryptophan	1999
Importance of barrier shape in enzyme-catalyzed reactions. Vibrationally assisted hydrogen tunneling in tryptophan tryptophylquinone-dependent amine dehydrogenases. The Journal of biological chemistry, 2001, Mar-02, Volume: 276, Issue:9 Topics: Benzylamines; Catalysis; Ethanolamine; Indolequinones; Oxidoreductases Acting on CH-NH Group Donors; Quinones; Tryptamines; Tryptophan; Vibration	2001
The covalent structure of the small subunit from Pseudomonas putida amine dehydrogenase reveals the presence of three novel types of internal cross-linkages, all involving cysteine in a thioether bond. The Journal of biological chemistry, 2001, Nov-16, Volume: 276, Issue:46 Topics: Amino Acid Sequence; Amino Acids; Cloning, Molecular; Cross-Linking Reagents; Cysteine; Glutamic Acid; Heme; Indolequinones; Mass Spectrometry; Models, Chemical; Models, Genetic; Molecular Sequence Data; Open Reading Frames; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Peptides; Protein Binding; Protein Processing, Post-Translational; Pseudomonas putida; Quinones; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Spectrometry, Mass, Electrospray Ionization; Sulfides; Tryptophan; X-Rays	2001
Active-site residues are critical for the folding and stability of methylamine dehydrogenase. Protein engineering, 2001, Volume: 14, Issue:9 Topics: Amino Acid Sequence; Binding Sites; Conserved Sequence; Crystallography; Disulfides; Enzyme Stability; Gene Expression Regulation, Bacterial; Hydrogen Bonding; Indolequinones; Kinetics; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Folding; Protein Processing, Post-Translational; Protein Structure, Secondary; Quinones; Rhodobacter sphaeroides; Sequence Alignment; Tryptophan	2001
Inter-subunit cross-linking of methylamine dehydrogenase by cyclopropylamine requires residue alphaPhe55. FEBS letters, 2002, Apr-24, Volume: 517, Issue:1-3 Topics: Cross-Linking Reagents; Cyclopropanes; Indolequinones; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Phenylalanine; Point Mutation; Protein Subunits; Quinones; Tryptophan	2002
Evidence for substrate activation of electron transfer from methylamine dehydrogenase to amicyanin. Journal of the American Chemical Society, 2003, Mar-19, Volume: 125, Issue:11 Topics: Bacterial Proteins; Binding Sites; Hydroquinones; Indolequinones; Kinetics; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Quinones; Tryptophan	2003
Catalysis and electron transfer in protein crystals: the binary and ternary complexes of methylamine dehydrogenase with electron acceptors. Biochimica et biophysica acta, 2003, Apr-11, Volume: 1647, Issue:1-2 Topics: Catalysis; Crystallization; Electron Spin Resonance Spectroscopy; Hydrogen-Ion Concentration; Indolequinones; Kinetics; Oxidoreductases Acting on CH-NH Group Donors; Quinones; Tryptophan	2003
Regioselectivity for condensation reactions of quinonoid models of tryptophan tryptophylquinone: a density functional theory study. The Journal of organic chemistry, 2003, May-02, Volume: 68, Issue:9 Topics: Chemical Phenomena; Chemistry, Physical; Indolequinones; Models, Theoretical; Molecular Structure; Structure-Activity Relationship; Thermodynamics; Tryptophan	2003
MauG, a novel diheme protein required for tryptophan tryptophylquinone biogenesis. Biochemistry, 2003, Jun-24, Volume: 42, Issue:24 Topics: Amino Acid Sequence; Cytochrome-c Peroxidase; Electron Spin Resonance Spectroscopy; Heme; Hemeproteins; Indolequinones; Molecular Sequence Data; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Sorting Signals; Quinones; Recombinant Proteins; Sequence Homology, Amino Acid; Spectrophotometry, Ultraviolet; Tryptophan	2003
Further insights into quinone cofactor biogenesis: probing the role of mauG in methylamine dehydrogenase tryptophan tryptophylquinone formation. Biochemistry, 2004, May-11, Volume: 43, Issue:18 Topics: Amino Acid Sequence; Chymotrypsin; Coenzymes; Cytochrome-c Peroxidase; Electrophoresis, Polyacrylamide Gel; Histidine; Hydrolysis; Indolequinones; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Processing, Post-Translational; Protein Subunits; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Trypsin; Tryptophan; Valine	2004
Active site aspartate residues are critical for tryptophan tryptophylquinone biogenesis in methylamine dehydrogenase. The Journal of biological chemistry, 2005, Apr-29, Volume: 280, Issue:17 Topics: Aspartic Acid; Binding Sites; Crystallography, X-Ray; Cysteine; Disulfides; Indolequinones; Kinetics; Mass Spectrometry; Methylamines; Models, Chemical; Models, Molecular; Models, Statistical; Mutation; Oxidoreductases Acting on CH-NH Group Donors; Oxygen; Paracoccus denitrificans; Protein Conformation; Tryptophan	2005
Cloning and characterization of histamine dehydrogenase from Nocardioides simplex. Archives of biochemistry and biophysics, 2005, Apr-01, Volume: 436, Issue:1 Topics: Amino Acid Sequence; Base Sequence; Cloning, Molecular; Flavins; Histamine; Hydrogen-Ion Concentration; Indolequinones; Iron-Sulfur Proteins; Kinetics; Molecular Sequence Data; Nocardiaceae; Oxidoreductases Acting on CH-NH Group Donors; Oxidoreductases, N-Demethylating; Sequence Alignment; Spectrum Analysis; Substrate Specificity; Thermodynamics; Tryptophan	2005
MauG-dependent in vitro biosynthesis of tryptophan tryptophylquinone in methylamine dehydrogenase. Journal of the American Chemical Society, 2005, Jun-15, Volume: 127, Issue:23 Topics: Hemeproteins; Indolequinones; Mass Spectrometry; Mutagenesis, Site-Directed; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Tryptophan	2005
Tryptophan tryptophylquinone cofactor biogenesis in the aromatic amine dehydrogenase of Alcaligenes faecalis. Cofactor assembly and catalytic properties of recombinant enzyme expressed in Paracoccus denitrificans. The FEBS journal, 2005, Volume: 272, Issue:22 Topics: Alcaligenes faecalis; Catalysis; Hydrogen-Ion Concentration; Indolequinones; Kinetics; Mass Spectrometry; Molecular Structure; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Recombinant Proteins; Tryptophan	2005
Evidence for redox cooperativity between c-type hemes of MauG which is likely coupled to oxygen activation during tryptophan tryptophylquinone biosynthesis. Biochemistry, 2006, Jan-24, Volume: 45, Issue:3 Topics: Bacterial Proteins; Electrochemistry; Heme; Indolequinones; Kinetics; Models, Molecular; Oxidation-Reduction; Oxygen; Paracoccus denitrificans; Tryptophan	2006
Isotope labeling studies reveal the order of oxygen incorporation into the tryptophan tryptophylquinone cofactor of methylamine dehydrogenase. Journal of the American Chemical Society, 2006, Sep-27, Volume: 128, Issue:38 Topics: Catalysis; Indolequinones; Isotope Labeling; Oxidoreductases Acting on CH-NH Group Donors; Oxygen; Oxygen Isotopes; Tryptophan	2006
Mechanistic possibilities in MauG-dependent tryptophan tryptophylquinone biosynthesis. Biochemistry, 2006, Nov-07, Volume: 45, Issue:44 Topics: Electrons; Electrophoresis, Polyacrylamide Gel; Hydrogen Peroxide; Indolequinones; Kinetics; Mass Spectrometry; Oxygen; Tryptophan	2006
Crystal structure of an electron transfer complex between aromatic amine dehydrogenase and azurin from Alcaligenes faecalis. Biochemistry, 2006, Nov-14, Volume: 45, Issue:45 Topics: Alcaligenes faecalis; Azurin; Crystallization; Crystallography, X-Ray; Electron Transport; Indolequinones; Models, Molecular; Oxidoreductases Acting on CH-NH Group Donors; Tryptophan	2006
Model studies of 6,7-indolequinone cofactors of quinoprotein amine dehydrogenases. The Journal of organic chemistry, 2007, Apr-27, Volume: 72, Issue:9 Topics: Alcohol Oxidoreductases; Amines; Aminophenols; Coenzymes; Crystallography, X-Ray; Dipeptides; Electrochemistry; Imines; Indolequinones; Molecular Structure; Quinones; Spectrophotometry, Infrared; Spectrophotometry, Ultraviolet; Structure-Activity Relationship; Tryptophan	2007
Catalysis by the isolated tryptophan tryptophylquinone-containing subunit of aromatic amine dehydrogenase is distinct from native enzyme and synthetic model compounds and allows further probing of TTQ mechanism. Biochemistry, 2008, Jan-08, Volume: 47, Issue:1 Topics: Amines; Benzylamines; Catalysis; Dimerization; Indolequinones; Kinetics; Models, Molecular; Molecular Structure; Oxidoreductases Acting on CH-NH Group Donors; Phenylhydrazines; Protein Subunits; Structure-Activity Relationship; Substrate Specificity; Tryptophan	2008
Kinetic and physical evidence that the diheme enzyme MauG tightly binds to a biosynthetic precursor of methylamine dehydrogenase with incompletely formed tryptophan tryptophylquinone. Biochemistry, 2008, Mar-04, Volume: 47, Issue:9 Topics: Bacterial Proteins; Chromatography, Gel; Indolequinones; Kinetics; Molecular Structure; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Binding; Tryptophan	2008
Structural comparison of crystal and solution states of the 138 kDa complex of methylamine dehydrogenase and amicyanin from Paracoccus versutus. Biochemistry, 2008, Jun-24, Volume: 47, Issue:25 Topics: Bacterial Proteins; Binding Sites; Catalysis; Copper; Crystallization; Crystallography, X-Ray; Electron Transport; Indolequinones; Kinetics; Metalloproteins; Methylamines; Models, Molecular; Molecular Weight; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Solutions; Tryptophan	2008
A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical. Proceedings of the National Academy of Sciences of the United States of America, 2008, Jun-24, Volume: 105, Issue:25 Topics: Bacterial Proteins; Catalysis; Free Radicals; Heme; Hemeproteins; Indolequinones; Iron; Paracoccus denitrificans; Protein Processing, Post-Translational; Spectroscopy, Mossbauer; Tryptophan	2008
Kinetic mechanism for the initial steps in MauG-dependent tryptophan tryptophylquinone biosynthesis. Biochemistry, 2009, Mar-24, Volume: 48, Issue:11 Topics: Bacterial Proteins; Hydrogen Peroxide; Indolequinones; Kinetics; Oxygen; Paracoccus denitrificans; Tryptophan	2009
Assignment of the vibrational spectra of enzyme-bound tryptophan tryptophyl quinones using a combined QM/MM approach. The journal of physical chemistry. A, 2010, Jan-21, Volume: 114, Issue:2 Topics: Biocatalysis; Catalytic Domain; Indolequinones; Models, Molecular; Molecular Conformation; Oxidoreductases Acting on CH-NH Group Donors; Quantum Theory; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman; Tryptophan; Vibration	2010
Biochemistry. Remote enzyme microsurgery. Science (New York, N.Y.), 2010, Mar-12, Volume: 327, Issue:5971 Topics: Catalytic Domain; Enzyme Precursors; Hemeproteins; Hydroxylation; Indolequinones; Models, Chemical; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Protein Binding; Protein Conformation; Protein Processing, Post-Translational; Tryptophan	2010
In crystallo posttranslational modification within a MauG/pre-methylamine dehydrogenase complex. Science (New York, N.Y.), 2010, Mar-12, Volume: 327, Issue:5971 Topics: Amino Acid Sequence; Bacterial Proteins; Biocatalysis; Catalytic Domain; Crystallography, X-Ray; Enzyme Precursors; Hemeproteins; Hydrogen Peroxide; Indolequinones; Ligands; Models, Molecular; Molecular Sequence Data; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Conformation; Protein Processing, Post-Translational; Tryptophan	2010
Long-range electron transfer reactions between hemes of MauG and different forms of tryptophan tryptophylquinone of methylamine dehydrogenase. Biochemistry, 2010, Jul-13, Volume: 49, Issue:27 Topics: Catalysis; Electron Transport; Electrons; Heme; Indolequinones; Kinetics; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Oxygen; Protein Processing, Post-Translational; Tryptophan	2010
The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesis. Biochemistry, 2011, Jan-11, Volume: 50, Issue:1 Topics: Bacterial Proteins; Binding Sites; Calcium; Indolequinones; Models, Molecular; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Structure, Secondary; Spectrophotometry; Spectrum Analysis, Raman; Tryptophan	2011
Crystal structures of CO and NO adducts of MauG in complex with pre-methylamine dehydrogenase: implications for the mechanism of dioxygen activation. Biochemistry, 2011, Apr-12, Volume: 50, Issue:14 Topics: Amino Acid Sequence; Bacterial Proteins; Binding Sites; Biocatalysis; Carbon Monoxide; Crystallography, X-Ray; Cytochrome-c Peroxidase; Ferrous Compounds; Glutamic Acid; Heme; Hemeproteins; Indolequinones; Models, Chemical; Models, Molecular; Molecular Sequence Data; Molecular Structure; Nitric Oxide; Oxidoreductases; Oxidoreductases Acting on CH-NH Group Donors; Oxygen; Paracoccus denitrificans; Protein Binding; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Spectrophotometry; Substrate Specificity; Tryptophan	2011
Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis. Proceedings of the National Academy of Sciences of the United States of America, 2011, Oct-11, Volume: 108, Issue:41 Topics: Amino Acid Substitution; Bacterial Proteins; Crystallography, X-Ray; Enzyme Precursors; Indolequinones; Models, Molecular; Multienzyme Complexes; Mutagenesis, Site-Directed; Mutant Proteins; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Processing, Post-Translational; Recombinant Proteins; Spectrophotometry; Tryptophan	2011
Proline 107 is a major determinant in maintaining the structure of the distal pocket and reactivity of the high-spin heme of MauG. Biochemistry, 2012, Feb-28, Volume: 51, Issue:8 Topics: Bacterial Proteins; Catalysis; Crystallography, X-Ray; Heme; Hemeproteins; Indolequinones; Kinetics; Ligands; Mass Spectrometry; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Oxygen; Paracoccus denitrificans; Proline; Tryptophan	2012
Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity. FEBS letters, 2012, Dec-14, Volume: 586, Issue:24 Topics: Bacterial Proteins; Heme; Heme-Binding Proteins; Hemeproteins; Histidine; Indolequinones; Ligands; Lysine; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Peroxides; Protein Processing, Post-Translational; Spectrophotometry; Tryptophan; Tyrosine	2012
Diradical intermediate within the context of tryptophan tryptophylquinone biosynthesis. Proceedings of the National Academy of Sciences of the United States of America, 2013, Mar-19, Volume: 110, Issue:12 Topics: Bacterial Proteins; Crystallography, X-Ray; Indolequinones; Mass Spectrometry; Oxidation-Reduction; Oxidoreductases; Paracoccus denitrificans; Substrate Specificity; Tryptophan	2013
A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis. FEBS letters, 2013, Jun-19, Volume: 587, Issue:12 Topics: Bacterial Proteins; Benzoquinones; Electron Transport; Enzyme Precursors; Indolequinones; Iron; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Binding; Protein Conformation; Tryptophan	2013
Tryptophan-mediated charge-resonance stabilization in the bis-Fe(IV) redox state of MauG. Proceedings of the National Academy of Sciences of the United States of America, 2013, Jun-11, Volume: 110, Issue:24 Topics: Catalysis; Enzyme Precursors; Ferric Compounds; Heme; Hemeproteins; Histidine; Indolequinones; Models, Chemical; Models, Molecular; Molecular Structure; Mutation; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Protein Processing, Post-Translational; Spectroscopy, Near-Infrared; Tryptophan; Tyrosine	2013
Structures of MauG in complex with quinol and quinone MADH. Acta crystallographica. Section F, Structural biology and crystallization communications, 2013, Volume: 69, Issue:Pt 7 Topics: Bacterial Proteins; Binding Sites; Crystallization; Crystallography, X-Ray; Indolequinones; Models, Molecular; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Conformation; Quinones; Tryptophan	2013
Carboxyl group of Glu113 is required for stabilization of the diferrous and bis-Fe(IV) states of MauG. Biochemistry, 2013, Sep-17, Volume: 52, Issue:37 Topics: Crystallography, X-Ray; Ferric Compounds; Ferrous Compounds; Glutamic Acid; Heme; Hemeproteins; Hydrogen Peroxide; Indolequinones; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Processing, Post-Translational; Tryptophan	2013
Mutation of Trp(93) of MauG to tyrosine causes loss of bound Ca(2+) and alters the kinetic mechanism of tryptophan tryptophylquinone cofactor biosynthesis. The Biochemical journal, 2013, Nov-15, Volume: 456, Issue:1 Topics: Bacterial Proteins; Calcium; Hemeproteins; Hydrogen Peroxide; Indolequinones; Kinetics; Mutation; Oxidation-Reduction; Paracoccus denitrificans; Protein Binding; Tryptophan; Tyrosine	2013
Probing bis-Fe(IV) MauG: experimental evidence for the long-range charge-resonance model. Angewandte Chemie (International ed. in English), 2015, Mar-16, Volume: 54, Issue:12 Topics: Amino Acid Substitution; Electron Spin Resonance Spectroscopy; Heme; Hemeproteins; Indolequinones; Models, Molecular; Oxidoreductases Acting on CH-NH Group Donors; Spectroscopy, Near-Infrared; Temperature; Tryptophan	2015
A T67A mutation in the proximal pocket of the high-spin heme of MauG stabilizes formation of a mixed-valent FeII/FeIII state and enhances charge resonance stabilization of the bis-FeIV state. Biochimica et biophysica acta, 2015, Volume: 1847, Issue:8 Topics: Bacterial Proteins; Crystallography, X-Ray; Electron Transport; Ferric Compounds; Ferrous Compounds; Heme; Hemeproteins; Indolequinones; Models, Molecular; Mutation; Oxidation-Reduction; Oxidoreductases Acting on CH-NH Group Donors; Paracoccus denitrificans; Protein Processing, Post-Translational; Rhodobacter sphaeroides; Spectrum Analysis, Raman; Tryptophan	2015
Ascorbate protects the diheme enzyme, MauG, against self-inflicted oxidative damage by an unusual antioxidant mechanism. The Biochemical journal, 2017, 07-17, Volume: 474, Issue:15 Topics: Antioxidants; Ascorbate Peroxidases; Ascorbic Acid; Bacterial Proteins; Crystallography, X-Ray; Heme; Hydrogen Peroxide; Hydroxyurea; Indolequinones; Iron; Kinetics; Mutant Proteins; Oxidation-Reduction; Oxidative Stress; Paracoccus denitrificans; Spectrum Analysis; Time Factors; Tryptophan	2017