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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...

Täydet tiedot

Tallennettuna:
Bibliografiset tiedot
Julkaisussa:Biochemistry
Päätekijät: Xia, Chuanwu, Rwere, Freeborn, Im, Sangchoul, Shen, Anna L., Waskell, Lucy, Kim, Jung-Ja P.
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: 2018
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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