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Effects of copper occupancy on the conformational landscape of peptidylglycine α-hydroxylating monooxygenase
The structures of metalloproteins that use redox-active metals for catalysis are usually exquisitely folded in a way that they are prearranged to accept their metal cofactors. Peptidylglycine α-hydroxylating monooxygenase (PHM) is a dicopper enzyme that catalyzes hydroxylation of the α-carbon of gly...
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| Опубликовано в: : | Commun Biol |
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| Главные авторы: | , , , , , , , , |
| Формат: | Artigo |
| Язык: | Inglês |
| Опубликовано: |
Nature Publishing Group UK
2018
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| Предметы: | |
| Online-ссылка: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6123673/ https://ncbi.nlm.nih.gov/pubmed/30271955 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s42003-018-0082-y |
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