Posttranslational Biosynthesis of the Protein-Derived Cofactor Tryptophan Tryptophylquinone

Proline 107 Is a Major Determinant in Maintaining the Structure of the Distal Pocket and Reactivity of the High-Spin Heme of MauG

(2012) Manliang Feng et al.   BIOCHEMISTRY

Characterization of Electron Tunneling and Hole Hopping Reactions between Different Forms of MauG and Methylamine Dehydrogenase within a Natural Protein Complex

(2012) Moonsung Choi et al.   BIOCHEMISTRY

Role of Calcium in Metalloenzymes: Effects of Calcium Removal on the Axial Ligation Geometry and Magnetic Properties of the Catalytic Diheme Center in MauG

(2012) Yan Chen et al.   BIOCHEMISTRY

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

(2012) Lyndal M. R. Jensen et al.   JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY

Crystal Structures of CO and NO Adducts of MauG in Complex with Pre-Methylamine Dehydrogenase: Implications for the Mechanism of Dioxygen Activation

(2011) Erik T. Yukl et al.   BIOCHEMISTRY

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

(2011) N. A. Tarboush et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Long-Range Electron Transfer Reactions between Hemes of MauG and Different Forms of Tryptophan Tryptophylquinone of Methylamine Dehydrogenase

(2010) Sooim Shin et al.   BIOCHEMISTRY

Functional Importance of Tyrosine 294 and the Catalytic Selectivity for the Bis-Fe(IV) State of MauG Revealed by Replacement of This Axial Heme Ligand with Histidine,

(2010) Nafez Abu Tarboush et al.   BIOCHEMISTRY

The Tightly Bound Calcium of MauG Is Required for Tryptophan Tryptophylquinone Cofactor Biosynthesis

(2010) Sooim Shin et al.   BIOCHEMISTRY

Unprecedented Fe(IV) Species in a Diheme Protein MauG: A Quantum Chemical Investigation on the Unusual Mössbauer Spectroscopic Properties

(2010) Yan Ling et al.   Journal of Physical Chemistry Letters

Generation of protein-derived redoxcofactors by posttranslational modification

(2010) Victor L. Davidson   Molecular BioSystems

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

(2010) L. M. R. Jensen et al.   SCIENCE

Suicide Inactivation of MauG during Reaction with O2or H2O2in the Absence of Its Natural Protein Substrate

(2009) Sooim Shin et al.   BIOCHEMISTRY

Kinetic Mechanism for the Initial Steps in MauG-Dependent Tryptophan Tryptophylquinone Biosynthesis†

(2009) Sheeyong Lee et al.   BIOCHEMISTRY

Heme Iron Nitrosyl Complex of MauG Reveals an Efficient Redox Equilibrium between Hemes with Only One Heme Exclusively Binding Exogenous Ligands

(2009) Rong Fu et al.   BIOCHEMISTRY

Review: Studies of ferric heme proteins with highly anisotropic/highly axial low spin (S= 1/2) electron paramagnetic resonance signals with bis-Histidine and histidine-methionine axial iron coordination

(2009) Giorgio Zoppellaro et al.   BIOPOLYMERS

Kinetic and Physical Evidence That the Diheme Enzyme MauG Tightly Binds to a Biosynthetic Precursor of Methylamine Dehydrogenase with Incompletely Formed Tryptophan Tryptophylquinone†

(2008) Xianghui Li et al.   BIOCHEMISTRY

Electron transfer in peptides and proteins

(2008) Bernd Giese et al.   CURRENT OPINION IN CHEMICAL BIOLOGY

A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical

(2008) X. Li et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA