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Double electron–electron resonance shows cytochrome P450cam undergoes a conformational change in solution upon binding substrate

Although cytochrome P450cam from Pseudomonas putida, the archetype for all heme monooxygenases, has long been known to have a closed active site, recent reports show that the enzyme can also be crystallized in at least two clusters of open conformations. This suggests that the enzyme may undergo sig...

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Detalhes bibliográficos
Main Authors: Stoll, Stefan, Lee, Young-Tae, Zhang, Mo, Wilson, Richard F., Britt, R. David, Goodin, David B.
Formato: Artigo
Idioma:Inglês
Publicado em: National Academy of Sciences 2012
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC3420169/
https://ncbi.nlm.nih.gov/pubmed/22826259
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1207123109
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