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Article

The structure of the yeast NADH dehydrogenase (Ndi1) reveals overlapping binding sites for water- and lipid-soluble substrates.

Proceedings of the National Academy of Sciences of the United States of America - 18 Sept 2012

Iwata Momi, Lee Yang, Yamashita Tetsuo, Yagi Takao, Iwata So, Cameron Alexander D, Maher Megan J

Abstract excerpt

Bioenergy is efficiently produced in the mitochondria by the respiratory system consisting of complexes I-V. In various organisms, complex I can be replaced by the alternative NADH-quinone oxidoreductase (NDH-2), which catalyzes the transfer of an electron from NADH via FAD to quinone, without proton pumping. The Ndi1 protein from Saccharomyces cerevisiae is a monotopic membrane protein, directed to the matrix. A...

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Identifiers

PMID: 22949654
DOI: 10.1073/pnas.1210059109
PMCID: PMC3458368

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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