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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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Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity

FEBS letters, 2012-12, Vol.586 (24), p.4339-4343

2012

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Properties of the high‐spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å away

FEBS letters, 2017-06, Vol.591 (11), p.1566-1572

2017

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Steady-state kinetic mechanism of LodA, a novel cysteine tryptophylquinone-dependent oxidase

FEBS letters, 2014-03, Vol.588 (5), p.752-756

2014

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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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Geometric and electronic structures of the His–Fe(IV)=O and His–Fe(IV)–Tyr hemes of MauG

Journal of biological inorganic chemistry, 2012-12, Vol.17 (8), p.1241-1255

2012

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A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis

FEBS letters, 2013-06, Vol.587 (12), p.1736-1741

2013

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X-ray structure of methanol dehydrogenase from Paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551i

Journal of biological inorganic chemistry, 2003-11, Vol.8 (8), p.843-854

2003

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Electron transfer in crystals of the binary and ternary complexes of methylamine dehydrogenase with amicyanin and cytochrome c551i as detected by EPR spectroscopy

Journal of biological inorganic chemistry, 2004-03, Vol.9 (2), p.231-237

2004

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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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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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Active-site residues are critical for the folding and stability of methylamine dehydrogenase

Protein engineering, 2001-09, Vol.14 (9), p.675-681

2001

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Measurement of the oxidation-reduction potentials of amicyanin and c-type cytochromes from Paracoccus denitrificans

FEBS letters, 1986-10, Vol.207 (2), p.239-242

1986

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Structure of an Electron Transfer Complex: Methylamine Dehydrogenase, Amicyanin, and Cytochrome c$_{551i}

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

1994

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Inter-subunit cross-linking of methylamine dehydrogenase by cyclopropylamine requires residue alphaPhe55

FEBS letters, 2002-04, Vol.517 (1-3), p.172

2002

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Inter-subunit cross-linking of methylamine dehydrogenase by cyclopropylamine requires residue αPhe55

FEBS letters, 2002-04, Vol.517 (1), p.172-174

2002

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Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase

FEBS letters, 1991-08, Vol.287 (1), p.163-166

1991

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Preliminary crystal structure studies of a ternary electron transfer complex between a quinoprotein, a blue copper protein, and a c‐type cytochrome

Protein science, 1993-02, Vol.2 (2), p.147-154

1993

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Factors affecting the stability of methanol dehydrogenase from Paracoccus denitrificans

FEMS microbiology letters, 1992-07, Vol.94 (1), p.53-57

1992

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Structure of an Electron Transfer Complex: Methylamine Dehydrogenase, Amicyanin, and Cytochrome c 551i

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

1994

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Cytochrome c-550 mediates electron transfer from inducible periplasmic c-type cytochromes to the cytoplasmic membrane of Paracoccus denitrificans

FEBS letters, 1989-03, Vol.245 (1), p.271-273

1989

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Factors affecting the stability of methanol dehydrogenase from Paracoccus denitrificans

FEMS microbiology letters, 1992-07, Vol.94 (1‐2), p.53-57

1992

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Evidence for two subclasses of methylamine dehydrogenases with distinct large subunits and conserved PQQ‐bearing small subunits

FEMS microbiology letters, 1987-09, Vol.44 (1), p.121-124

1987

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Crystallization and preliminary X-ray crystallographic study of the quinoprotein methanol dehydrogenase from bacterium W3A1

FEBS letters, 1989-11, Vol.258 (1), p.175-176

1989

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Road maps to achieve glycemic control in type 2 diabetes mellitus: ACE/AACE Diabetes Road Map Task Force

Endocrine practice, 2007-05, Vol.13 (3), p.260-268

2007

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

Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity

Properties of the high‐spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å away

Steady-state kinetic mechanism of LodA, a novel cysteine tryptophylquinone-dependent oxidase

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

Geometric and electronic structures of the His–Fe(IV)=O and His–Fe(IV)–Tyr hemes of MauG

A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis

X-ray structure of methanol dehydrogenase from Paracoccus denitrificans and molecular modeling of its interactions with cytochrome c-551i

Electron transfer in crystals of the binary and ternary complexes of methylamine dehydrogenase with amicyanin and cytochrome c551i as detected by EPR spectroscopy

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

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

Active-site residues are critical for the folding and stability of methylamine dehydrogenase

Measurement of the oxidation-reduction potentials of amicyanin and c-type cytochromes from Paracoccus denitrificans

Structure of an Electron Transfer Complex: Methylamine Dehydrogenase, Amicyanin, and Cytochrome c$_{551i}

Inter-subunit cross-linking of methylamine dehydrogenase by cyclopropylamine requires residue alphaPhe55

Inter-subunit cross-linking of methylamine dehydrogenase by cyclopropylamine requires residue αPhe55

Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase

Preliminary crystal structure studies of a ternary electron transfer complex between a quinoprotein, a blue copper protein, and a c‐type cytochrome

Factors affecting the stability of methanol dehydrogenase from Paracoccus denitrificans

Structure of an Electron Transfer Complex: Methylamine Dehydrogenase, Amicyanin, and Cytochrome c 551i

Cytochrome c-550 mediates electron transfer from inducible periplasmic c-type cytochromes to the cytoplasmic membrane of Paracoccus denitrificans

Factors affecting the stability of methanol dehydrogenase from Paracoccus denitrificans

Evidence for two subclasses of methylamine dehydrogenases with distinct large subunits and conserved PQQ‐bearing small subunits

Crystallization and preliminary X-ray crystallographic study of the quinoprotein methanol dehydrogenase from bacterium W3A1

Road maps to achieve glycemic control in type 2 diabetes mellitus: ACE/AACE Diabetes Road Map Task Force

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