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Article

Tryptophan-mediated charge-resonance stabilization in the bis-Fe(IV) redox state of MauG.

Proceedings of the National Academy of Sciences of the United States of America - 11 Jun 2013

Geng Jiafeng, Dornevil Kednerlin, Davidson Victor L, Liu Aimin

Abstract excerpt

The diheme enzyme MauG catalyzes posttranslational modifications of a methylamine dehydrogenase precursor protein to generate a tryptophan tryptophylquinone cofactor. The MauG-catalyzed reaction proceeds via a bis-Fe(IV) intermediate in which one heme is present as Fe(IV)=O and the other as Fe(IV) with axial histidine and tyrosine ligation. Herein, a unique near-infrared absorption feature exhibited specifically...

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Identifiers

PMID: 23720312
DOI: 10.1073/pnas.1301544110
PMCID: PMC3683780

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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