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Structural Adaptability Facilitates Histidine Heme Ligation in a Cytochrome P450
[Image: see text] Almost all known members of the cytochrome P450 (CYP) superfamily conserve a key cysteine residue that coordinates the heme iron. Although mutation of this residue abolishes monooxygenase activity, recent work has shown that mutation to either serine or histidine unlocks non-natura...
Autores principales: | McIntosh, John A., Heel, Thomas, Buller, Andrew R., Chio, Linda, Arnold, Frances H. |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2015
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4635421/ https://www.ncbi.nlm.nih.gov/pubmed/26299431 http://dx.doi.org/10.1021/jacs.5b07107 |
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