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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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| Main Authors: | , , , , , |
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| Formáid: | Artigo |
| Teanga: | Inglês |
| Foilsithe: |
National Academy of Sciences
2012
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| Ábhair: | |
| Rochtain Ar Líne: | 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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