ArticleThe Biochemical journal2013
Investigating the function of [2Fe-2S] cluster N1a, the off-pathway cluster in complex I, by manipulating its reduction potential.
Article in The Biochemical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
26 citing papers in PubMed, 57 citations in OpenAlex.
- Probing the Role of Accessory Domains in Oxygen Stability of [FeFe]-Hydrogenases.Journal of the American Chemical Society · 2026Article
- Post-catalysis structures of mitochondrial complex I with ubiquinol-10 bound in the active site.Nature communications · 2026Article
- Crystal Structure of a Thioredoxin-like Ferredoxin Encoded Within a Cobalamin Biosynthetic Operon of Rhodobacter capsulatus.The protein journal · 2025Article
- Subunits E-F-G of E. coli Complex I can form an active complex when expressed alone, but in time-delayed assembly co-expression of B-CD-E-F-G is optimal.Biochimica et biophysica acta. Bioenergetics · 2022Article
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- In Silico Identification and Characterization of a Hypothetical Protein FromBioinformatics and biology insights · 2022Article
- Is there a special relationship between complex I activity and nigral neuronal loss in Parkinson's disease? A critical reappraisal.Brain research · 2021Review
- Structure ofeLife · 2021Article
- Paracoccus denitrificans: a genetically tractable model system for studying respiratory complex I.Scientific reports · 2021Article
- Mechanisms of Mitochondrial ROS Production in Assisted Reproduction: The Known, the Unknown, and the Intriguing.Antioxidants (Basel, Switzerland) · 2020Review
- Article
- A mechanism to prevent production of reactive oxygen species by Escherichia coli respiratory complex I.Nature communications · 2019Article
- Energetics and Dynamics of Proton-Coupled Electron Transfer in the NADH/FMN Site of Respiratory Complex I.Journal of the American Chemical Society · 2019Article
- Long-range proton-coupled electron transfer in biological energy conversion: towards mechanistic understanding of respiratory complex I.Journal of the Royal Society, Interface · 2018Review
- Low cost, microcontroller based heating device for multi-wavelength differential scanning fluorimetry.Scientific reports · 2018Article
- Reduction of the off-pathway iron-sulphur cluster N1a of Escherichia coli respiratory complex I restrains NADScientific reports · 2017Article
- Article
- Article
- Ischemic A/D transition of mitochondrial complex I and its role in ROS generation.Biochimica et biophysica acta · 2016Review
- Energy conversion, redox catalysis and generation of reactive oxygen species by respiratory complex I.Biochimica et biophysica acta · 2016Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
nadhquinone oxidoreductase (complex I) couples NADH oxidation and quinone reduction to proton translocation across an energy-transducing membrane. All complexes I contain a flavin to oxidize NADH, seven iron-sulfur clusters to transfer electrons from the flavin to quinone and an eighth cluster (N1a) on the opposite side of the flavin. The role of cluster N1a is unknown, but Escherichia coli complex I has an unusually high-potential cluster N1a and its reduced flavin produces H2O2, not superoxide, suggesting that cluster N1a may affect reactive oxygen species production. In the present study, we combine protein film voltammetry with mutagenesis in overproduced N1a-binding subunits to identify two residues that switch N1a between its high- (E. coli, valine and asparagine) and low- (Bos taurus and Yarrowia lipolytica, proline and methionine) potential forms. The mutations were incorporated into E. coli complex I: cluster N1a could no longer be reduced by NADH, but H2O2 and superoxide production were unaffected. The reverse mutations (that increase the potential by ~0.16 V) were incorporated into Y. lipolytica complex I, but N1a was still not reduced by NADH. We conclude that cluster N1a does not affect reactive oxygen species production by the complex I flavin; it is probably required for enzyme assembly or stability.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.