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The role of the proximal cysteine hydrogen bonding interaction in cytochrome P450 2B4 studied by cryoreduction/EPR/ENDOR spectroscopy
Crystallographic studies have shown that the F429H mutation of cytochrome P450 2B4 introduces an H-bond between His 429 and the proximal thiolate ligand, Cys 436, without altering the protein fold but sharply decreases the enzymatic activity and stabilizes the oxyferrous P450 2B4 complex. To charact...
Tallennettuna:
| Julkaisussa: | Biochemistry |
|---|---|
| Päätekijät: | , , , , , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
2016
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4834902/ https://ncbi.nlm.nih.gov/pubmed/26750753 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.biochem.5b00744 |
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