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Issue 9, 2013
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MauG: a di-heme enzyme required for methylamine dehydrogenase maturation

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Abstract

Methylamine dehydrogenase (MADH) requires the cofactor tryptophan tryptophylquinone (TTQ) for activity. TTQ is a posttranslational modification that results from an 8-electron oxidation of two specific tryptophans in the MADH β-subunit. The final 6-electron oxidation is catalyzed by an unusual c-type di-heme enzyme, MauG. The di-ferric enzyme can react with H2O2, but atypically for c-type hemes the di-ferrous enzyme can react with O2 as well. In both cases, an unprecedented bis-Fe(IV) redox state is formed, composed of a ferryl heme (Fe(IV)[double bond, length as m-dash]O) with the second heme as Fe(IV) stabilized by HisTyr axial ligation. Bis-Fe(IV) MauG acts as a potent 2-electron oxidant. Catalysis is long-range and requires a hole hopping electron transfer mechanism. This review highlights the current knowledge and focus of research into this fascinating system.

Graphical abstract: MauG: a di-heme enzyme required for methylamine dehydrogenase maturation

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Publication details

The article was received on 05 Sep 2012, accepted on 12 Oct 2012 and first published on 16 Oct 2012


Article type: Perspective
DOI: 10.1039/C2DT32059B
Citation: Dalton Trans., 2013,42, 3127-3135
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    MauG: a di-heme enzyme required for methylamine dehydrogenase maturation

    C. M. Wilmot and E. T. Yukl, Dalton Trans., 2013, 42, 3127
    DOI: 10.1039/C2DT32059B

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