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Ambidentate H-bonding of NO and O(2) in Heme Proteins
The affinity and reactivity of the gaseous molecules CO, NO and O(2) (XO) in heme protein adducts are controlled by secondary interactions, especially by H-bonds donated from distal protein residues. Vibrational spectroscopy, supported by DFT modeling, has revealed that for NO and O(2), but not for...
Tallennettuna:
| Päätekijät: | , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
2012
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3463650/ https://ncbi.nlm.nih.gov/pubmed/22824153 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jinorgbio.2012.05.013 |
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