Cargando…
Coupling of Redox and Structural States in Cytochrome P450 Reductase Studied by Molecular Dynamics Simulation
Cytochrome P450 reductase (CPR) is the key protein that regulates the electron transfer from NADPH to various heme-containing monooxygenases. CPR has two flavin-containing domains: one with flavin adenine dinucleotide (FAD), called FAD domain, and the other with flavin mononucleotide (FMN), called F...
Autores principales: | Iijima, Mikuru, Ohnuki, Jun, Sato, Takato, Sugishima, Masakazu, Takano, Mitsunori |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6597723/ https://www.ncbi.nlm.nih.gov/pubmed/31249341 http://dx.doi.org/10.1038/s41598-019-45690-2 |
Ejemplares similares
-
Crystal structures of hydroxymethylbilane synthase complexed with a substrate analog: a single substrate-binding site for four consecutive condensation steps
por: Sato, Hideaki, et al.
Publicado: (2021) -
Liver microsomal lipid enhances the activity and redox coupling of colocalized cytochrome P450 reductase‐cytochrome P450 3A4 in nanodiscs
por: Liu, Kang‐Cheng, et al.
Publicado: (2017) -
Redox-Linked Domain Movements in the Catalytic Cycle of Cytochrome P450 Reductase
por: Huang, Wei-Cheng, et al.
Publicado: (2013) -
Conformational Equilibrium of NADPH–Cytochrome P450 Oxidoreductase Is Essential for Heme Oxygenase Reaction
por: Sugishima, Masakazu, et al.
Publicado: (2020) -
The FMN “140s Loop” of Cytochrome P450 Reductase Controls Electron Transfer to Cytochrome P450
por: Rwere, Freeborn, et al.
Publicado: (2021)