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Coupling between oxidation state and hydrogen bond conformation in heme proteins
In all heme proteins for which crystal structures are available, the N(ε) of a histidyl residue is bonded to the heme iron and N(δ) is hydrogen bonded to a carbonyl oxygen of the peptide backbone. We investigate here the possibility that a change in oxidation state of the iron or a change in the geo...
Tallennettuna:
| Päätekijät: | , , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
1979
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC383176/ https://ncbi.nlm.nih.gov/pubmed/220604 |
| Tagit: |
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