The carboxyl group of Glu113 is required for stabilization of the diferrous and bis-Fe(IV) states of MauG

Samankaltaisia teoksia

• Functional importance of Tyrosine294 and the catalytic selectivity for the bis-Fe(IV) state of MauG revealed by replacement of this axial heme ligand with Histidine,
  Tekijä: Tarboush, Nafez Abu, et al.
  Julkaistu: (2010)
• A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesis
  Tekijä: Tarboush, Nafez Abu, et al.
  Julkaistu: (2013)
• Long Range Electron Transfer Reactions between Hemes of MauG and Different Forms of Tryptophan Tryptophylquinone of Methylamine Dehydrogenase
  Tekijä: Shin, Sooim, et al.
  Julkaistu: (2010)
• Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis
  Tekijä: Tarboush, Nafez Abu, et al.
  Julkaistu: (2011)
• A T67A mutation in the proximal pocket of the high-spin heme of MauG stabilizes formation of a mixed-valent Fe(II)/Fe(III) state and enhances charge resonance stabilization of the bis-Fe(IV) state
  Tekijä: Shin, Sooim, et al.
  Julkaistu: (2015)