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Trp–His covalent adduct in bilirubin oxidase is crucial for effective bilirubin binding but has a minor role in electron transfer
Unlike any protein studied so far, the active site of bilirubin oxidase from Myrothecium verrucaria contains a unique type of covalent link between tryptophan and histidine side chains. The role of this post-translational modification in substrate binding and oxidation is not sufficiently understood...
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| Vydáno v: | Sci Rep |
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| Hlavní autoři: | , , , , , , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Nature Publishing Group UK
2019
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6757100/ https://ncbi.nlm.nih.gov/pubmed/31548583 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41598-019-50105-3 |
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