ArticleBiochemistry2012
Mössbauer spectroscopy on respiratory complex I: the iron-sulfur cluster ensemble in the NADH-reduced enzyme is partially oxidized.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 57 citations in OpenAlex.
- Lessons, connections, hypotheses and predictions from protein film electrochemistry.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026Review
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- TheMolecules (Basel, Switzerland) · 2025Review
- Respiratory complex IIIbioRxiv : the preprint server for biology · 2025Article
- Undulating Free Energy Landscapes Buffer Redox Chains from Environmental Fluctuations.The journal of physical chemistry. B · 2024Article
- Mechanism of rotenone binding to respiratory complex I depends on ligand flexibility.Scientific reports · 2023Article
- Single protonation of the reduced quinone in respiratory complex I drives four-proton pumping.FEBS letters · 2023Article
- Structure of respiratory complex I - An emerging blueprint for the mechanism.Current opinion in structural biology · 2022Review
- Functional basis of electron transport within photosynthetic complex I.Nature communications · 2021Article
- Aerobic Respiration: Criticism of the Proton-centric Explanation Involving Rotary Adenosine Triphosphate Synthesis, Chemiosmosis Principle, Proton Pumps and Electron Transport Chain.Biochemistry insights · 2018Article
- Reduction of the off-pathway iron-sulphur cluster N1a of Escherichia coli respiratory complex I restrains NADScientific reports · 2017Article
- Article
- Energy conversion, redox catalysis and generation of reactive oxygen species by respiratory complex I.Biochimica et biophysica acta · 2016Review
- A giant molecular proton pump: structure and mechanism of respiratory complex I.Nature reviews. Molecular cell biology · 2015Review
- Electron tunneling rates in respiratory complex I are tuned for efficient energy conversion.Angewandte Chemie (International ed. in English) · 2015Article
- Multi-haem cytochromes in Shewanella oneidensis MR-1: structures, functions and opportunities.Journal of the Royal Society, Interface · 2015Review
- The mechanism of coupling between electron transfer and proton translocation in respiratory complex I.Journal of bioenergetics and biomembranes · 2014Review
- Investigating the function of [2Fe-2S] cluster N1a, the off-pathway cluster in complex I, by manipulating its reduction potential.The Biochemical journal · 2013Article
- Semiquinone and cluster N6 signals in His-tagged proton-translocating NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli.The Journal of biological chemistry · 2013Article
- Nuclear resonance vibrational spectroscopy reveals the FeS cluster composition and active site vibrational properties of an OChemical scienceArticle
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3 authors at 1 institution in 1 country.
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Abstract
In mitochondria, complex I (NADH:quinone oxidoreductase) couples electron transfer to proton translocation across an energy-transducing membrane. It contains a flavin mononucleotide to oxidize NADH, and an unusually long series of iron-sulfur (FeS) clusters that transfer the electrons to quinone. Understanding electron transfer in complex I requires spectroscopic and structural data to be combined to reveal the properties of individual clusters and of the ensemble. EPR studies on complex I from Bos taurus have established that five clusters (positions 1, 2, 3, 5, and 7 along the seven-cluster chain extending from the flavin) are (at least partially) reduced by NADH. The other three clusters, positions 4 and 6 plus a cluster on the other side of the flavin, are not observed in EPR spectra from the NADH-reduced enzyme: they may remain oxidized, have unusual or coupled spin states, or their EPR signals may be too fast relaxing. Here, we use Mössbauer spectroscopy on (57)Fe-labeled complex I from the mitochondria of Yarrowia lipolytica to show that the cluster ensemble is only partially reduced in the NADH-reduced enzyme. The three EPR-silent clusters are oxidized, and only the terminal 4Fe cluster (position 7) is fully reduced. Together with the EPR analyses, our results reveal an alternating profile of higher and lower potential clusters between the two active sites in complex I; they are not consistent with the consensus picture of a set of isopotential clusters. The implications for intramolecular electron transfer along the extended chain of cofactors in complex I are discussed.
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