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Article

Site-directed mutagenesis of Gln103 reveals the influence of this residue on the redox properties and stability of MauG.

Biochemistry - 4 Mar 2014

Shin Sooim, Yukl Erik T, Sehanobish Esha, Wilmot Carrie M, Davidson Victor L

Abstract excerpt

The diheme enzyme MauG catalyzes a six-electron oxidation that is required for the posttranslational modification of a precursor of methylamine dehydrogenase (preMADH) to complete the biosynthesis of its protein-derived cofactor, tryptophan tryptophylquinone (TTQ). Crystallographic and computational studies have implicated Gln103 in stabilizing the Fe(IV)═O moiety of the bis-Fe(IV) state by hydrogen bonding. The...

Topics

Crystallography, X-Ray
Enzyme Stability
Glutamine
Hemeproteins
Iron
Models, Molecular
Mutagenesis, Site-Directed
Mutation
Oxidation-Reduction
Paracoccus denitrificans
Protein Conformation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 24517455
DOI: 10.1021/bi5000349
PMCID: PMC3985960

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Site-directed mutagenesis of Gln103 reveals the influence of this residue on the redox properties and stability of MauG.PMID 24517455Read ↗

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