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Tryptophan-mediated charge-resonance stabilization in the bis-Fe(IV) redox state of MauG

Proceedings of the National Academy of Sciences - PNAS, 2013-06, Vol.110 (24), p.9639-9644

2013

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Roles of Conserved Residues of the Glycine Oxidase GoxA in Controlling Activity, Cooperativity, Subunit Composition, and Cysteine Tryptophylquinone Biosynthesis

The Journal of biological chemistry, 2016-10, Vol.291 (44), p.23199-23207

2016

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In Crystallo Posttranslational Modification Within a MauG/Pre-Methylamine Dehydrogenase Complex

Science (American Association for the Advancement of Science), 2010-03, Vol.327 (5971), p.1392-1394

2010

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Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis

Proceedings of the National Academy of Sciences - PNAS, 2011-10, Vol.108 (41), p.16956-16961

2011

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Diradical intermediate within the context of tryptophan tryptophylquinone biosynthesis

Proceedings of the National Academy of Sciences - PNAS, 2013-03, Vol.110 (12), p.4569-4573

2013

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A Catalytic Di-Heme bis-Fe(IV) Intermediate, Alternative to an Fe(IV)=O Porphyrin Radical

Proceedings of the National Academy of Sciences - PNAS, 2008-06, Vol.105 (25), p.8597-8600

2008

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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 - PNAS, 2015-09, Vol.112 (35), p.10896-10901

2015

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Roles of active-site residues in catalysis, substrate binding, cooperativity, and the reaction mechanism of the quinoprotein glycine oxidase

The Journal of biological chemistry, 2020-05, Vol.295 (19), p.6472-6481

2020

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Kinetic and structural evidence that Asp-678 plays multiple roles in catalysis by the quinoprotein glycine oxidase

The Journal of biological chemistry, 2019-11, Vol.294 (46), p.17463-17470

2019

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The hemerythrin-like diiron protein from Mycobacterium kansasii is a nitric oxide peroxidase

The Journal of biological chemistry, 2022-03, Vol.298 (3), p.101696-101696, Article 101696

2022

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The Rv2633c protein of Mycobacterium tuberculosis is a non-heme di-iron catalase with a possible role in defenses against oxidative stress

The Journal of biological chemistry, 2018-02, Vol.293 (5), p.1590-1595

2018

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Metabolomics reveals critical adrenergic regulatory checkpoints in glycolysis and pentose–phosphate pathways in embryonic heart

The Journal of biological chemistry, 2018-05, Vol.293 (18), p.6925-6941

2018

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Involvement of a Putative [Fe-S]-cluster-binding Protein in the Biogenesis of Quinohemoprotein Amine Dehydrogenase

The Journal of biological chemistry, 2006-05, Vol.281 (19), p.13672-13684

2006

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Structure of an electron transfer complex : methylamine dehydrogenase amicyanin, and cytochrome C551i

Science (American Association for the Advancement of Science), 1994-04, Vol.264 (5155), p.86-90

1994

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An Engineered CuA Amicyanin Capable of Intermolecular Electron Transfer Reactions

The Journal of biological chemistry, 2003-11, Vol.278 (47), p.47269-47274

2003

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Active Site Aspartate Residues Are Critical for Tryptophan Tryptophylquinone Biogenesis in Methylamine Dehydrogenase

The Journal of biological chemistry, 2005-04, Vol.280 (17), p.17392-17396

2005

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Use of Indirect Site-directed Mutagenesis to Alter the Substrate Specificity of Methylamine Dehydrogenase

The Journal of biological chemistry, 2002-02, Vol.277 (6), p.4119-4122

2002

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Active site aspartate residues are critical for tryptophan tryptophylquinone biogenesis in methylamine dehydrogenase

The Journal of biological chemistry, 2005-04, Vol.280 (17), p.17392-17396

2005

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Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis -Fe IV state of MauG

Proceedings of the National Academy of Sciences - PNAS, 2015-09, Vol.112 (35), p.10896-10901

2015

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Resolving the mechanism of glycine oxidation by GoxA using X‐ray crystallography

The FASEB journal, 2018-04, Vol.32 (S1), p.655.31-655.31

2018

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Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of thebis-FeIVstate of MauG

Proceedings of the National Academy of Sciences - PNAS, 2015-09, Vol.112 (35), p.10896-10901

2015

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Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-Fe^sup IV^ state of MauG

Proceedings of the National Academy of Sciences - PNAS, 2015-09, Vol.112 (35), p.10896

2015

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Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-Fe super( IV) state of MauG

Proceedings of the National Academy of Sciences - PNAS, 2015-09, Vol.112 (35), p.10896-10896

2015

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Crystal structure analysis of amicyanin and apoamicyanin from paracoccus denitrificans at 2.0 Å and 1.8 Å resolution

Protein science, 1993-05, Vol.2 (5), p.739-752

1993

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Gated and Ungated Electron Transfer Reactions from Aromatic Amine Dehydrogenase to Azurin

The Journal of biological chemistry, 1999-10, Vol.274 (41), p.29081-29086

1999

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Tryptophan-mediated charge-resonance stabilization in the bis-Fe(IV) redox state of MauG

Roles of Conserved Residues of the Glycine Oxidase GoxA in Controlling Activity, Cooperativity, Subunit Composition, and Cysteine Tryptophylquinone Biosynthesis

In Crystallo Posttranslational Modification Within a MauG/Pre-Methylamine Dehydrogenase Complex

Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis

Diradical intermediate within the context of tryptophan tryptophylquinone biosynthesis

A Catalytic Di-Heme bis-Fe(IV) Intermediate, Alternative to an Fe(IV)=O Porphyrin Radical

Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-FeIV state of MauG

Roles of active-site residues in catalysis, substrate binding, cooperativity, and the reaction mechanism of the quinoprotein glycine oxidase

Kinetic and structural evidence that Asp-678 plays multiple roles in catalysis by the quinoprotein glycine oxidase

The hemerythrin-like diiron protein from Mycobacterium kansasii is a nitric oxide peroxidase

The Rv2633c protein of Mycobacterium tuberculosis is a non-heme di-iron catalase with a possible role in defenses against oxidative stress

Metabolomics reveals critical adrenergic regulatory checkpoints in glycolysis and pentose–phosphate pathways in embryonic heart

Involvement of a Putative [Fe-S]-cluster-binding Protein in the Biogenesis of Quinohemoprotein Amine Dehydrogenase

Structure of an electron transfer complex : methylamine dehydrogenase amicyanin, and cytochrome C551i

An Engineered CuA Amicyanin Capable of Intermolecular Electron Transfer Reactions

Active Site Aspartate Residues Are Critical for Tryptophan Tryptophylquinone Biogenesis in Methylamine Dehydrogenase

Use of Indirect Site-directed Mutagenesis to Alter the Substrate Specificity of Methylamine Dehydrogenase

Active site aspartate residues are critical for tryptophan tryptophylquinone biogenesis in methylamine dehydrogenase

Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis -Fe IV state of MauG

Resolving the mechanism of glycine oxidation by GoxA using X‐ray crystallography

Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of thebis-FeIVstate of MauG

Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-Fe^sup IV^ state of MauG

Roles of multiple-proton transfer pathways and proton-coupled electron transfer in the reactivity of the bis-Fe super( IV) state of MauG

Crystal structure analysis of amicyanin and apoamicyanin from paracoccus denitrificans at 2.0 Å and 1.8 Å resolution

Gated and Ungated Electron Transfer Reactions from Aromatic Amine Dehydrogenase to Azurin

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