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Histidine Orientation Modulates the Structure and Dynamics of a de Novo Metalloenzyme Active Site
The ultrafast dynamics of a de novo metalloenzyme active site is monitored using two-dimensional infrared spectroscopy. The homotrimer of parallel, coiled coil α-helices contains a His(3)-Cu(I) metal site where CO is bound and serves as a vibrational probe of the hydrophobic interior of the self-ass...
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| Publicado no: | J Am Chem Soc |
|---|---|
| Main Authors: | , , , , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2015
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5250509/ https://ncbi.nlm.nih.gov/pubmed/26247178 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/jacs.5b02840 |
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