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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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Библиографические подробности
Опубликовано в: :Commun Biol
Главные авторы: Maheshwari, Sweta, Shimokawa, Chizu, Rudzka, Katarzyna, Kline, Chelsey D., Eipper, Betty A., Mains, Richard E., Gabelli, Sandra B., Blackburn, Ninian, Amzel, L. Mario
Формат: Artigo
Язык:Inglês
Опубликовано: Nature Publishing Group UK 2018
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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