Ubiquinone binding site of yeast NADH dehydrogenase revealed by structures binding novel competitive- and mixed-type inhibitors

Yeast Ndi1 is a monotopic alternative NADH dehydrogenase. Its crystal structure in complex with the electron acceptor, ubiquinone, has been determined. However, there has been controversy regarding the ubiquinone binding site. To address these points, we identified the first competitive inhibitor of...

وصف كامل

محفوظ في:
التفاصيل البيبلوغرافية
الحاوية / القاعدة:Sci Rep
المؤلفون الرئيسيون: Yamashita, Tetsuo, Inaoka, Daniel Ken, Shiba, Tomoo, Oohashi, Takumi, Iwata, So, Yagi, Takao, Kosaka, Hiroaki, Miyoshi, Hideto, Harada, Shigeharu, Kita, Kiyoshi, Hirano, Katsuya
التنسيق: Artigo
اللغة:Inglês
منشور في: Nature Publishing Group UK 2018
الموضوعات:
Article
الوصول للمادة أونلاين:https://ncbi.nlm.nih.gov/pmc/articles/PMC5799168/
https://ncbi.nlm.nih.gov/pubmed/29402945
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41598-018-20775-6
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