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Structural and kinetic studies of Asp632 mutants and fully-reduced NADPH-cytochrome P450 oxidoreductase define the role of Asp632 loop dynamics in control of NADPH binding and hydride transfer
Conformational changes of NADPH-cytochrome P450 oxidoreductase (CYPOR) associated with electron transfer from NADPH to electron acceptors via FAD and FMN have been investigated through structural studies of the 4-electron-reduced NADP(+)-bound enzyme and kinetic and structural studies of mutants aff...
Tallennettuna:
| Julkaisussa: | Biochemistry |
|---|---|
| Päätekijät: | , , , , , |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
2018
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| Aiheet: | |
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5967631/ https://ncbi.nlm.nih.gov/pubmed/29308883 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.biochem.7b01102 |
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