ReviewJournal of bioenergetics and biomembranes2014
Essential regions in the membrane domain of bacterial complex I (NDH-1): the machinery for proton translocation.
Review in Journal of bioenergetics and biomembranes, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Global conformations ofScience advances · 2025Article
- Comparative Transcriptomics Reveals Distinct Adaptation Mechanisms for Degradation ofMicroorganisms · 2025Article
- Proteomic analysis reveals the roles of silicon in mitigating glyphosate-induced toxicity in Brassica napus L.Scientific reports · 2025Article
- Investigation of hydrated channels and proton pathways in a high-resolution cryo-EM structure of mammalian complex I.Science advances · 2023Article
- Membrane-domain mutations in respiratory complex I impede catalysis but do not uncouple proton pumping from ubiquinone reduction.PNAS nexus · 2022Article
- Paracoccus denitrificans: a genetically tractable model system for studying respiratory complex I.Scientific reports · 2021Article
- Role of water and protein dynamics in proton pumping by respiratory complex I.Scientific reports · 2017Article
- Conserved amino acid residues of the NuoD segment important for structure and function of Escherichia coli NDH-1 (complex I).Biochemistry · 2015Article
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
Abstract
The proton-translocating NADH-quinone oxidoreductase (complex I/NDH-1) is the first and largest enzyme of the respiratory chain which has a central role in cellular energy production and is implicated in many human neurodegenerative diseases and aging. It is believed that the peripheral domain of complex I/NDH-1 transfers the electron from NADH to Quinone (Q) and the redox energy couples the proton translocation in the membrane domain. To investigate the mechanism of the proton translocation, in a series of works we have systematically studied all membrane subunits in the Escherichia coli NDH-1 by site-directed mutagenesis. In this mini-review, we have summarized our strategy and results of the mutagenesis by depicting residues essential for proton translocation, along with those for subunit connection. It is suggested that clues to understanding the driving forces of proton translocation lie in the similarities and differences of the membrane subunits, highlighting the communication of essential charged residues among the subunits. A possible proton translocation mechanism with all membrane subunits operating in unison is described.
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