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Article

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

Scientific reports - 5 Feb 2018

Yamashita Tetsuo, Inaoka Daniel Ken, Shiba Tomoo, Oohashi Takumi, Iwata So, Yagi Takao, Kosaka Hiroaki, Miyoshi Hideto, Harada Shigeharu, Kita Kiyoshi, Hirano Katsuya

Abstract excerpt

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 Ndi1, stigmatellin, along with new mixed-type inhibitors, AC0-12 and myxothiazol, and thereby determined the...

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Identifiers

PMID: 29402945
DOI: 10.1038/s41598-018-20775-6
PMCID: PMC5799168

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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