| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10337813 | Journal of Molecular Graphics and Modelling | 2011 | 5 Pages |
Abstract
⺠The enzyme studied (PhnI) is able to interact with PAH in more efficient way than similar others. ⺠For the first time it is shown that PhnI structure is characterized by numerous intermolecular channels. ⺠The PAH interaction with the enzyme depends not only by the number of aromatic rings but also by the PAH shape that results critical in predicting their biodegradation suitability.
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Physical Sciences and Engineering
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Physical and Theoretical Chemistry
Authors
Vito Librando, Matteo Pappalardo,