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Pearson Arwen R.
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http://hub.abes.fr/acs/periodical/bichaw/2003/volume_42/issue_11/101021bi027073a/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/2007/volume_46/issue_28/101021bi700086r/authorship/1
http://hub.abes.fr/acs/periodical/bichaw/2006/volume_45/issue_44/101021bi061497d/authorship/3
http://hub.abes.fr/acs/periodical/bichaw/2003/volume_42/issue_24/101021bi034243q/authorship/4
http://hub.abes.fr/acs/periodical/bichaw/2004/volume_43/issue_18/101021bi049863l/authorship/1
http://hub.abes.fr/acs/periodical/jacsat/2006/volume_128/issue_38/101021ja064466e/authorship/1
http://hub.abes.fr/acs/periodical/jacsat/2005/volume_127/issue_23/101021ja051734k/authorship/4
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Mechanistic Possibilities in MauG-Dependent Tryptophan TryptophylquinoneBiosynthesis
Isotope Labeling Studies Reveal the Order of Oxygen Incorporation into theTryptophan Tryptophylquinone Cofactor of Methylamine Dehydrogenase
Further Insights into Quinone Cofactor Biogenesis: Probing the Role of mauG inMethylamine Dehydrogenase Tryptophan Tryptophylquinone Formation
The Crystal Structure of Cytochrome P460 of Nitrosomonas europaea Reveals aNovel Cytochrome Fold and Heme−Protein Cross-link,
MauG, a Novel Diheme Protein Required for Tryptophan TryptophylquinoneBiogenesis
Understanding Quinone Cofactor Biogenesis in Methylamine Dehydrogenasethrough Novel Cofactor Generation
MauG-Dependent in Vitro Biosynthesis of Tryptophan Tryptophylquinone inMethylamine Dehydrogenase
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