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S K-edge XAS and DFT Calculations on Cytochrome P450: Covalent and Ionic Contributions to the Cysteine-Fe Bond and Their Contribution to Reactivity
Experimental covalencies of the Fe-S bond for the resting low-spin and substrate-bound high-spin active site of cytochrome P450 are reported. DFT calculations on the active site indicate that one H-bonding interaction from the protein backbone is needed to reproduce the experimental values. The H-bo...
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| Hauptverfasser: | , , , , , |
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| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
2009
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2734335/ https://ncbi.nlm.nih.gov/pubmed/19438234 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/ja901868q |
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