ArticleFEBS letters2010
A new hypothesis on the simultaneous direct and indirect proton pump mechanisms in NADH-quinone oxidoreductase (complex I).
Article in FEBS letters, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 45 citations in OpenAlex.
- Molecular Dynamics Simulation of T10609C and C10676G Mutations of MitochondrialBioinformatics and biology insights · 2020Article
- Long-range proton-coupled electron transfer in biological energy conversion: towards mechanistic understanding of respiratory complex I.Journal of the Royal Society, Interface · 2018Review
- Symmetry-related proton transfer pathways in respiratory complex I.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Mrp Antiporters Have Important Roles in Diverse Bacteria and Archaea.Frontiers in microbiology · 2017Review
- A giant molecular proton pump: structure and mechanism of respiratory complex I.Nature reviews. Molecular cell biology · 2015Review
- On the mechanism of respiratory complex I.Journal of bioenergetics and biomembranes · 2014Review
- Randomly selected suppressor mutations in genes for NADH : quinone oxidoreductase-1, which rescue motility of a Salmonella ubiquinone-biosynthesis mutant strain.Microbiology (Reading, England) · 2014Article
- Article
- Mitochondrial complex I and cell death: a semi-automatic shotgun model.Cell death & disease · 2011Review
- Article
- Tracing the trail of protons through complex I of the mitochondrial respiratory chain.PLoS biology · 2011Article
- A model of the proton translocation mechanism of complex I.The Journal of biological chemistry · 2011Article
- Mutagenesis of the L, M, and N subunits of Complex I from Escherichia coli indicates a common role in function.PloS one · 2011Article
- Positive Darwinian selection in the piston that powers proton pumps in complex I of the mitochondria of Pacific salmon.PloS one · 2011Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Recently, Sazanov's group reported the X-ray structure of whole complex I [Nature, 465, 441 (2010)], which presented a strong clue for a "piston-like" structure as a key element in an "indirect" proton pump. We have studied the NuoL subunit which has a high sequence similarity to Na(+)/H(+) antiporters, as do the NuoM and N subunits. We constructed 27 site-directed NuoL mutants. Our data suggest that the H(+)/e(-) stoichiometry seems to have decreased from (4H(+)/2e(-)) in the wild-type to approximately (3H(+)/2e(-)) in NuoL mutants. We propose a revised hypothesis that each of the "direct" and the "indirect" proton pumps transports 2H(+) per 2e(-).
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