دورية أكاديمية
Kinetic and docking studies of the interaction of quinones with the quinone reductase active site.
| العنوان: | Kinetic and docking studies of the interaction of quinones with the quinone reductase active site. |
|---|---|
| المؤلفون: | Zhou, Zhigang, Fisher, Derek, Spidel, Jared, Greenfield, Jodi, Patson, Brian J., MD, Fazal, Aleem, Wigal, Carl, Moe, Owen A, Madura, Jeffry D |
| المصدر: | Department of Medicine |
| بيانات النشر: | LVHN Scholarly Works |
| سنة النشر: | 2003 |
| المجموعة: | Lehigh Valley Health Network: LVHN Scholarly Works |
| مصطلحات موضوعية: | Animals, Anthraquinones, Benzoquinones, Binding Sites, Flavins, Humans, Kinetics, Models, Chemical, Molecular, NAD(P)H Dehydrogenase (Quinone), Naphthoquinones, Rats, Structure-Activity Relationship, Substrate Specificity, Thermodynamics, Tyrosine, Department of Medicine, Medicine and Health Sciences |
| الوصف: | NAD(P)H/quinone acceptor oxidoreductase type 1 (QR1) protects cells from cytotoxic and neoplastic effects of quinones though two-electron reduction. Kinetic experiments, docking, and binding affinity calculations were performed on a series of structurally varied quinone substrates. A good correlation between calculated and measured binding affinities from kinetic determinations was obtained. The experimental and theoretical studies independently support a model in which quinones (with one to three fused aromatic rings) bind in the QR1 active site utilizing a pi-stacking interaction with the isoalloxazine ring of the FAD cofactor. |
| نوع الوثيقة: | text |
| اللغة: | unknown |
| العلاقة: | https://scholarlyworks.lvhn.org/medicine/5403Test; https://pubmed.ncbi.nlm.nih.gov/12590585Test/ |
| الإتاحة: | https://scholarlyworks.lvhn.org/medicine/5403Test https://pubmed.ncbi.nlm.nih.gov/12590585Test/ |
| رقم الانضمام: | edsbas.29EB1176 |
| قاعدة البيانات: | BASE |
| الوصف غير متاح. |