ReviewAnnual review of biochemistry2013
Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone.
Review in Annual review of biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 36 citations in OpenAlex.
- Insights into the Thermodynamics and Kinetics of Amino-Acid Radicals in Proteins.Annual review of biophysics · 2022Review
- Oxidative Crosslinking of Peptides and Proteins: Mechanisms of Formation, Detection, Characterization and Quantification.Molecules (Basel, Switzerland) · 2021Review
- Computing Proton-Coupled Redox Potentials of Fluorotyrosines in a Protein Environment.The journal of physical chemistry. B · 2021Article
- The Uniqueness of Tryptophan in Biology: Properties, Metabolism, Interactions and Localization in Proteins.International journal of molecular sciences · 2020Review
- Moving Through Barriers in Science and Life.Annual review of biochemistry · 2019Article
- Diversity of structures, catalytic mechanisms and processes of cofactor biosynthesis of tryptophylquinone-bearing enzymes.Archives of biochemistry and biophysics · 2018Review
- Ascorbate protects the diheme enzyme, MauG, against self-inflicted oxidative damage by an unusual antioxidant mechanism.The Biochemical journal · 2017Article
- Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å away.FEBS letters · 2017Article
- Roles of Copper and a Conserved Aspartic Acid in the Autocatalytic Hydroxylation of a Specific Tryptophan Residue during Cysteine Tryptophylquinone Biogenesis.Biochemistry · 2017Article
- A Suicide Mutation Affecting Proton Transfers to High-Valent Hemes Causes Inactivation of MauG during Catalysis.Biochemistry · 2016Article
- Mechanism of protein oxidative damage that is coupled to long-range electron transfer to high-valent haems.The Biochemical journal · 2016Article
- Interaction of GoxA with Its Modifying Enzyme and Its Subunit Assembly Are Dependent on the Extent of Cysteine Tryptophylquinone Biosynthesis.Biochemistry · 2016Article
- Converting the bis-FeIV state of the diheme enzyme MauG to Compound I decreases the reorganization energy for electron transfer.The Biochemical journal · 2016Article
- Electron flow through biological molecules: does hole hopping protect proteins from oxidative damage?Quarterly reviews of biophysics · 2015Review
- Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-FeIV state of MauG.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- 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 · 2015Article
- Could tyrosine and tryptophan serve multiple roles in biological redox processes?Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2015Article
- Mechanisms for control of biological electron transfer reactions.Bioorganic chemistry · 2014Review
- Photochemical tyrosine oxidation in the structurally well-defined α3Y protein: proton-coupled electron transfer and a long-lived tyrosine radical.Journal of the American Chemical Society · 2014Article
- A simple method to engineer a protein-derived redox cofactor for catalysis.Biochimica et biophysica acta · 2014Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Methylamine dehydrogenase (MADH) catalyzes the oxidative deamination of methylamine to formaldehyde and ammonia. Tryptophan tryptophylquinone (TTQ) is the protein-derived cofactor of MADH required for this catalytic activity. TTQ is biosynthesized through the posttranslational modification of two tryptophan residues within MADH, during which the indole rings of two tryptophan side chains are cross-linked and two oxygen atoms are inserted into one of the indole rings. MauG is a c-type diheme enzyme that catalyzes the final three reactions in TTQ formation. In total, this is a six-electron oxidation process requiring three cycles of MauG-dependent two-electron oxidation events using either H2O2 or O2. The MauG redox form responsible for the catalytic activity is an unprecedented bis-Fe(IV) species. The amino acids of MADH that are modified are ≈ 40 Å from the site where MauG binds oxygen, and the reaction proceeds by a hole hopping electron transfer mechanism. This review addresses these highly unusual aspects of the long-range catalytic reaction mediated by MauG.
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