ArticleFEBS letters2012
Effects of the loss of the axial tyrosine ligand of the low-spin heme of MauG on its physical properties and reactivity.
Article in FEBS letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- A Stable Ferryl Porphyrin at the Active Site of Y463M BthA.Journal of the American Chemical Society · 2020Article
- Towards the understanding of the enzymatic cleavage of polyisoprene by the dihaem-dioxygenase RoxA.AMB Express · 2019Article
- Heterolytic OO bond cleavage: Functional role of Glu113 during bis-Fe(IV) formation in MauG.Journal of inorganic biochemistry · 2017Article
- Article
- A T67A mutation in the proximal pocket of the high-spin heme of MauG stabilizes formation of a mixed-valent FeII/FeIII state and enhances charge resonance stabilization of the bis-FeIV state.Biochimica et biophysica acta · 2015Article
- Probing bis-Fe(IV) MauG: experimental evidence for the long-range charge-resonance model.Angewandte Chemie (International ed. in English) · 2015Article
- Bis-Fe(IV): nature's sniper for long-range oxidation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Review
- Site-directed mutagenesis of Gln103 reveals the influence of this residue on the redox properties and stability of MauG.Biochemistry · 2014Article
- MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis.Archives of biochemistry and biophysics · 2014Review
- Carboxyl group of Glu113 is required for stabilization of the diferrous and bis-Fe(IV) states of MauG.Biochemistry · 2013Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
MauG catalyzes posttranslational modifications of methylamine dehydrogenase to complete the biosynthesis of its protein-derived tryptophan tryptophylquinone (TTQ) cofactor. MauG possesses a five-coordinate high-spin and a six-coordinate low-spin ferric heme, the latter with His-Tyr ligation. Replacement of this tyrosine with lysine generates a MauG variant with only high-spin ferric heme and altered spectroscopic and redox properties. Y294K MauG cannot stabilize the bis-Fe(IV) redox state required for TTQ biosynthesis but instead forms a compound I-like species on reaction with peroxide. The results clarify the role of Tyr ligation of the five-coordinate heme in determining the physical and redox properties and reactivity of MauG.
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