ArticleBiochemistry2015
Conserved amino acid residues of the NuoD segment important for structure and function of Escherichia coli NDH-1 (complex I).
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Selective inhibition of respiratory complex I reveals a bioenergetic vulnerability inbioRxiv : the preprint server for biology · 2026Article
- Quinone chemistry in respiratory complex I involves protonation of a conserved aspartic acid residue.FEBS letters · 2024Article
- Mechanistic Principles of Hydrogen Evolution in the Membrane-Bound Hydrogenase.Journal of the American Chemical Society · 2024Article
- Article
- Respiratory complex I with charge symmetry in the membrane arm pumps protons.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Biochemical consequences of two clinically relevant ND-gene mutations in Escherichia coli respiratory complex I.Scientific reports · 2021Article
- Ubiquinone Binding and Reduction by Complex I-Open Questions and Mechanistic Implications.Frontiers in chemistry · 2021Review
- Structure of inhibitor-bound mammalian complex I.Nature communications · 2020Article
- How inter-subunit contacts in the membrane domain of complex I affect proton transfer energetics.Biochimica et biophysica acta. Bioenergetics · 2018Article
- Long-range proton-coupled electron transfer in biological energy conversion: towards mechanistic understanding of respiratory complex I.Journal of the Royal Society, Interface · 2018Review
- Correlating kinetic and structural data on ubiquinone binding and reduction by respiratory complex I.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Terminal Electron-Proton Transfer Dynamics in the Quinone Reduction of Respiratory Complex I.Journal of the American Chemical Society · 2017Article
- Energy conversion, redox catalysis and generation of reactive oxygen species by respiratory complex I.Biochimica et biophysica acta · 2016Review
- A Self-Assembled Respiratory Chain that Catalyzes NADH Oxidation by Ubiquinone-10 Cycling between Complex I and the Alternative Oxidase.Angewandte Chemie (International ed. in English) · 2016Article
- Genome Analysis of Structure-Function Relationships in Respiratory Complex I, an Ancient Bioenergetic Enzyme.Genome biology and evolution · 2015Article
- Redox-induced activation of the proton pump in the respiratory complex I.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
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9 authors.
Funding
Abstract
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 the homologous DNA recombination technique to clarify the role of selected key amino acid residues of the NuoD segment. Among them, residues Tyr273 and His224 were considered candidates for having important interactions with the quinone headgroup. Mutant Y273F retained partial activity but lost sensitivity to capsaicin-40. Mutant H224R scarcely affected the activity, suggesting that this residue may not be essential. His224 is located in a loop near the N-terminus of the NuoD segment (Gly217-Phe227) which is considered to form part of the quinone binding cavity. In contrast to the His224 mutation, mutants G217V, P218A, and G225V almost completely lost the activity. One region of this loop is positioned close to a cytosolic loop of the NuoA subunit in the membrane domain, and together they seem to be important in keeping the quinone binding cavity intact. The structural role of the longest helix in the NuoD segment located behind the quinone binding cavity was also investigated. Possible roles of other highly conserved residues of the NuoD segment are discussed.
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