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Site-Directed Mutagenesis of Gln103 Reveals the Influence of This Residue on the Redox Properties and Stability of MauG
[Image: see text] 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...
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| 主要な著者: | , , , , |
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| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
American
Chemical Society
2014
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| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3985960/ https://ncbi.nlm.nih.gov/pubmed/24517455 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi5000349 |
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