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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...
Αποθηκεύτηκε σε:
| Κύριοι συγγραφείς: | , , , , , |
|---|---|
| Μορφή: | Artigo |
| Γλώσσα: | Inglês |
| Έκδοση: |
National Academy of Sciences
2012
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| Θέματα: | |
| Διαθέσιμο Online: | 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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