Trp57 is modified and covalently bonded to the sidechain of Trp108 to form a cofactor, tryptophan tryptophylquinone (TTQ). Amicyanin (Swiss-prot;P22364) is a primary acceptor, whilst cytochrome c (Swiss-prot;P29899) is a secondary acceptor. Thus, this enzyme catalyzes the following reactions (see [30], [37]): (A) Exchange of double-bonded atoms (carbonyl bond by amine; Schiff-base formation), releasing H2O: (B) Isomerization (shift of double-bond position): (C) Exchange of double-bonded atoms (Schiff-base deformation by water), giving aldehyde product and aminoquinol TTQ: (D) Electron transfer from aminoquinol TTQ to copper of the primary acceptor protein, amicyanin, leading to formation of aminosemiquinone TTQ: (E) Exchange of double-bonded atoms (Schiff-base deformation by water), giving TTQ and ammonia: The transferred electron is transferred further to Heme group of the secondary acceptor, cytochrome c.
Electron Transport Ethylamine Dehydrogenase
amine: (acceptor) oxidoreductase (deaminating)
primary-amine:(acceptor) oxidoreductase (deaminating)
TRP 57;TRP 108(Tryptophan tryptophylquinone)
TRQ 57;TRP 107(Tryptophan tryptophylquinone)
TRQ 57;TRP 108(Tryptophan tryptophylquinone)
TRW 57;TRP 108(Tryptophan tryptophylquinone-phenylhydrazine)
Colworth Medal Lecture. Enzymes in the quantum world.
Active-site residues are critical for the folding and stability of methylamine dehydrogenase.
Use of indirect site-directed mutagenesis to alter the substrate specificity of methylamine dehydrogenase.
Purification, crystallization and preliminary X-ray investigation of quinoprotein methylamine dehydrogenase from Thiobacillus versutus.
Preliminary X-ray crystallographic studies of methylamine dehydrogenase and methylamine dehydrogenase--amicyanin complexes from Paracoccus denitrificans.
Structure of quinoprotein methylamine dehydrogenase at 2.25 A resolution.
Structure determination of quinoprotein methylamine dehydrogenase from Thiobacillus versutus.
Cloning and sequencing of the structural gene for the small subunit of methylamine dehydrogenase from Methylobacterium extorquens AM1: evidence for two tryptophan residues involved in the active center.
Methylamine oxidase from Arthrobacter P1 as a prototype of eukaryotic plasma amine oxidase and diamine oxidase.
Inhibition by cyclopropylamine of the quinoprotein methylamine dehydrogenase is mechanism-based and causes covalent cross-linking of alpha and beta subunits.
Direct electrochemistry of the enzyme, methylamine dehydrogenase, from bacterium W3A1.
Crystallographic investigations of the tryptophan-derived cofactor in the quinoprotein methylamine dehydrogenase.
A new cofactor in a prokaryotic enzyme: tryptophan tryptophylquinone as the redox prosthetic group in methylamine dehydrogenase.
The genetic organization of the mau gene cluster of the facultative autotroph Paracoccus denitrificans.
X-RAY CRYSTALLOGRAPHY OF COMPLEX WITH AMICYANIN
Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin.
Reactions of benzylamines with methylamine dehydrogenase. Evidence for a carbanionic reaction intermediate and reaction mechanism similar to eukaryotic quinoproteins.
Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor.
Three-dimensional structure of the quinoprotein methylamine dehydrogenase from Paracoccus denitrificans determined by molecular replacement at 2.8 A resolution.
Preliminary crystal structure studies of a ternary electron transfer complex between a quinoprotein, a blue copper protein, and a c-type cytochrome.
Kinetic and thermodynamic analysis of a physiologic intermolecular electron-transfer reaction between methylamine dehydrogenase and amicyanin.
Kinetics of the reduction of wild-type and mutant cytochrome c-550 by methylamine dehydrogenase and amicyanin from Thiobacillus versutus.
Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i.
Binding of monovalent cations to methylamine dehydrogenase in the semiquinone state and its effect on electron transfer.
Evidence for a methylammonium-binding site on methylamine dehydrogenase of Thiobacillus versutus.
Electron transfer from copper to heme within the methylamine dehydrogenase--amicyanin--cytochrome c-551i complex.
Electrostatic environment of the tryptophylquinone cofactor in methylamine dehydrogenase: evidence from resonance Raman spectroscopy of model compounds.
Enzymatic and electron transfer activities in crystalline protein complexes.
Catalytic role of monovalent cations in the mechanism of proton transfer which gates an interprotein electron transfer reaction.
Factors which stabilize the methylamine dehydrogenase-amicyanin electron transfer protein complex revealed by site-directed mutagenesis.
Crystallographic and spectroscopic studies of native, aminoquinol, and monovalent cation-bound forms of methylamine dehydrogenase from Methylobacterium extorquens AM1.
Redox properties of tryptophan tryptophylquinone enzymes. Correlation with structure and reactivity.
Refined crystal structure of methylamine dehydrogenase from Paracoccus denitrificans at 1.75 A resolution.
Identification of a new reaction intermediate in the oxidation of methylamine dehydrogenase by amicyanin.
Amperometric detection of histamine with a methylamine dehydrogenase polypyrrole-based sensor.
Molecular basis for complex formation between methylamine dehydrogenase and amicyanin revealed by inverse mutagenesis of an interprotein salt bridge.
Conversion of methylamine dehydrogenase to a long-chain amine dehydrogenase by mutagenesis of a single residue.
Characterization of the Tryptophyl-Semiquinone Catalytic Intermediate of Methylamine Dehydrogenase by Electron Spin-Echo Envelope Modulation Spectroscopy.
Methylamine dehydrogenase. Structure and function of electron transfer complexes.
Re-engineering monovalent cation binding sites of methylamine dehydrogenase: effects on spectral properties and gated electron transfer.
QM/MM studies show substantial tunneling for the hydrogen-transfer reaction in methylamine dehydrogenase.
Importance of barrier shape in enzyme-catalyzed reactions. Vibrationally assisted hydrogen tunneling in tryptophan tryptophylquinone-dependent amine dehydrogenases.
Mutation of alphaPhe55 of methylamine dehydrogenase alters the reorganization energy and electronic coupling for its electron transfer reaction with amicyanin.
A new conceptual framework for enzyme catalysis. Hydrogen tunnelling coupled to enzyme dynamics in flavoprotein and quinoprotein enzymes.
Probing mechanisms of catalysis and electron transfer by methylamine dehydrogenase by site-directed mutagenesis of alpha Phe55.
Catalysis and electron transfer in protein crystals: the binary and ternary complexes of methylamine dehydrogenase with electron acceptors.
Direct dynamics calculations of reaction rate and kinetic isotope effects in enzyme catalysed reactions.
Evidence for substrate activation of electron transfer from methylamine dehydrogenase to amicyanin.