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...

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Detalles Bibliográficos
Autores principales: McIntosh, John A., Heel, Thomas, Buller, Andrew R., Chio, Linda, Arnold, Frances H.
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

Internet

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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