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Article

Conserved amino acid residues of the NuoD segment important for structure and function of Escherichia coli NDH-1 (complex I).

Biochemistry - 27 Jan 2015

Sinha Prem Kumar, Castro-Guerrero Norma, Patki Gaurav, Sato Motoaki, Torres-Bacete Jesus, Sinha Subhash, Miyoshi Hideto, Matsuno-Yagi Akemi, Yagi Takao

Abstract excerpt

The NuoD segment (homologue of mitochondrial 49 kDa subunit) of the proton-translocating NADH:quinone oxidoreductase (complex I/NDH-1) from Escherichia coli is in the hydrophilic domain and bears many highly conserved amino acid residues. The three-dimensional structural model of NDH-1 suggests that the NuoD segment, together with the neighboring subunits, constitutes a putative quinone binding cavity. We used...

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PMID: 25545070
DOI: 10.1021/bi501403t
PMCID: PMC4310626

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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