Ascorbate protects the diheme enzyme, MauG, against self-inflicted oxidative damage by an unusual antioxidant mechanism
Author:
Affiliation:
1. Burnett School of Biomedical Sciences, College of Medicine, University of Central Florida, 6900 Lake Nona Blvd, Orlando, FL 32827, U.S.A.
Abstract
Publisher
Portland Press Ltd.
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
https://portlandpress.com/biochemj/article-pdf/474/15/2563/689693/bcj-2017-0349.pdf
Reference36 articles.
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2. Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone;Davidson;Annu. Rev. Biochem.,2013
3. Further insights into quinone cofactor biogenesis: probing the role of MauG in methylamine dehydrogenase TTQ formation;Pearson;Biochemistry,2004
4. Pyrroloquinoline quinone (PQQ) from methanol dehydrogenase and tryptophan tryptophylquinone (TTQ) from methylamine dehydrogenase;Davidson;Adv. Protein Chem.,2001
5. A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical;Li;Proc. Natl Acad. Sci. U.S.A.,2008
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