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Structure of a quinohemoprotein amine dehydrogenase with an uncommon redox cofactor and highly unusual crosslinking
The crystal structure of the heterotrimeric quinohemoprotein amine dehydrogenase from Paracoccus denitrificans has been determined at 2.05-Å resolution. Within an 82-residue subunit is contained an unusual redox cofactor, cysteine tryptophylquinone (CTQ), consisting of an orthoquinone-modified trypt...
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| Hlavní autoři: | , , , , , , , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
The National Academy of Sciences
2001
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC64671/ https://ncbi.nlm.nih.gov/pubmed/11717396 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.241429098 |
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