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biochemistry & molecular biology (57) 57
methylamine dehydrogenase (55) 55
tryptophan (53) 53
index medicus (47) 47
tryptophan - analogs & derivatives (47) 47
oxidation-reduction (36) 36
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heme (29) 29
bacterial proteins - metabolism (28) 28
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oxidoreductases acting on ch-nh group donors - chemistry (26) 26
tryptophan tryptophylquinone biosynthesis (26) 26
paracoccus denitrificans - enzymology (25) 25
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post-translational modification (17) 17
crystallography, x-ray (16) 16
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maug (16) 16
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paracoccus denitrificans - metabolism (13) 13
quinone (13) 13
amino acid sequence (12) 12
multidisciplinary sciences (12) 12
oxidation (12) 12
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paracoccus denitrificans - genetics (12) 12
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oxidoreductases acting on ch-nh group donors - genetics (11) 11
posttranslational modification (11) 11
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Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2011, Volume 108, Issue 41, pp. 16956 - 16961
The diheme enzyme MauG catalyzes the posttranslational modification of the precursor protein of methylamine dehydrogenase (preMADH) to complete biosynthesis of... 
Quinones | Hydroquinones | Dehydrogenases | Electron transfer | Atoms | Electron tunneling | Biosynthesis | Biochemistry | Oxidation | Kinetics | Cytochrome | Peroxidase | Protein oxidation | Protein radical | Electron hopping | OXYGEN ACTIVATION | MULTIFREQUENCY EPR | MECHANISM | peroxidase | MULTIDISCIPLINARY SCIENCES | protein radical | METHYLAMINE DEHYDROGENASE | electron hopping | cytochrome | REDUCTION | HEME | BIOGENESIS | protein oxidation | PROTEINS | ELECTRON-TRANSFER REACTIONS | Bacterial Proteins - chemistry | Indolequinones - biosynthesis | Multienzyme Complexes - metabolism | Tryptophan - chemistry | Crystallography, X-Ray | Tryptophan - analogs & derivatives | Recombinant Proteins - metabolism | Mutagenesis, Site-Directed | Enzyme Precursors - chemistry | Oxidation-Reduction | Tryptophan - genetics | Bacterial Proteins - genetics | Mutant Proteins - genetics | Oxidoreductases Acting on CH-NH Group Donors - chemistry | Models, Molecular | Recombinant Proteins - chemistry | Mutant Proteins - metabolism | Multienzyme Complexes - genetics | Oxidoreductases Acting on CH-NH Group Donors - metabolism | Recombinant Proteins - genetics | Multienzyme Complexes - chemistry | Enzyme Precursors - metabolism | Tryptophan - biosynthesis | Mutant Proteins - chemistry | Bacterial Proteins - metabolism | Protein Processing, Post-Translational | Paracoccus denitrificans - genetics | Spectrophotometry | Paracoccus denitrificans - enzymology | Amino Acid Substitution | Post-translational modification | Physiological aspects | Tryptophan | Research | Mutagenesis | Heme | Index Medicus | OXIDATION | TRYPTOPHAN | CATALYSIS | ELECTRON TRANSFER | MUTAGENESIS | PRECURSOR | METHYLAMINE | BASIC BIOLOGICAL SCIENCES | CRYSTAL STRUCTURE | IRON | BENZOQUINONES | 60 APPLIED LIFE SCIENCES | MODIFICATIONS | BIOSYNTHESIS | ENZYMES | MUTATIONS | RESIDUES | OXIDOREDUCTASES | Biological Sciences
Journal Article
Journal Article
Journal Article
Biochemistry, ISSN 0006-2960, 11/2006, Volume 45, Issue 44, pp. 13276 - 13283
Journal Article
FEBS Letters, ISSN 0014-5793, 06/2013, Volume 587, Issue 12, pp. 1736 - 1741
Journal Article
Biochemical Journal, ISSN 0264-6021, 11/2013, Volume 456, Issue 1, pp. 129 - 137
Mutagenesis of Trp93 of the dihaem enzyme MauG revealed a role for this residue in binding Ca2+ and created an enzyme that exhibits an extraordinarily long... 
Electron transfer | MauG | Haem | Tryptophan tryptopylquinone | Protein radical | Methylamine dehydrogenase precursor
Journal Article
BIOCHEMICAL JOURNAL, ISSN 0264-6021, 11/2013, Volume 456, pp. 129 - 137
The dihaem enzyme MauG catalyses a six-electron oxidation required for post-translational modification of preMADH (precursor of methylamine dehydrogenase) to... 
SPIN HEME | MauG | MUTAGENESIS | DIFFERENT FORMS | DI-HEME PEROXIDASES | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | protein radical | METHYLAMINE DEHYDROGENASE | tryptophan tryptopylquinone | methylamine dehydrogenase precursor | haem | electron transfer | STRUCTURAL BASIS | INTERMEDIATE | CYTOCHROME-C PEROXIDASE | LIGAND
Journal Article
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, ISSN 1433-7851, 03/2015, Volume 54, Issue 12, pp. 3692 - 3696
The biosynthesis of tryptophan tryptophylquinone, a protein-derived cofactor, involves a long-range reaction mediated by a bis-Fe-IV intermediate of a diheme... 
SPIN HEME | OXIDATION | near-infrared spectroscopy | heme proteins | AROMATIC CATION-RADICALS | METHYLAMINE DEHYDROGENASE | METHIONINE RESIDUES | CHEMISTRY, MULTIDISCIPLINARY | charge resonance | ELECTRON-TRANSFER | REACTION CENTERS | KINETICS | electronic structure | high-valence iron | TRYPTOPHAN TRYPTOPHYLQUINONE BIOSYNTHESIS | CYANIDE
Journal Article