Crystal structure of the entire respiratory complex I
Open accessAbstract
Complex I is the first and largest enzyme of the respiratory chain and has a central role in cellular energy production through the coupling of NADH:ubiquinone electron transfer to proton translocation. It is also implicated in many common human neurodegenerative diseases. Here, we report the first crystal structure of the entire, intact complex I (from Thermus thermophilus) at 3.3 Å resolution. The structure of the 536-kDa complex comprises 16 different subunits, with a total of 64 transmembrane helices and 9 iron-sulphur clusters. The core fold of subunit Nqo8 (ND1 in humans) is, unexpectedly, similar to a half-channel of the antiporter-like subunits. Small subunits nearby form a linked second half-channel, which completes the fourth proton-translocation pathway (present in addition to the channels in three antiporter-like subunits). The quinone-binding site is unusually long, narrow and enclosed. The quinone headgroup binds at the deep end of this chamber, near iron-sulphur cluster N2. Notably, the chamber is linked to the fourth channel by a 'funnel' of charged residues. The link continues over the entire membrane domain as a flexible central axis of charged and polar residues, and probably has a leading role in the propagation of conformational changes, aided by coupling elements. The structure suggests that a unique, out-of-the-membrane quinone-reaction chamber enables the redox energy to drive concerted long-range conformational changes in the four antiporter-like domains, resulting in translocation of four protons per cycle.
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The model shows Cys39 is at the hinge region of complex I facing the mitochondrial matrix, adjacent to the half-channel element of one proposed proton translocation pathway and close to the ubiquinone binding pocket.
“Our model shows that Cys39 is located at the hinge region of complex I facing the mitochondrial matrix. Furthermore, Cys39 is adjacent to the half-channel element of one of the four proposed proton translocation pathways of complex I and is close to the ubiquinone binding pocket, where ubiquinone receives electrons from the N2 iron-sulfur center (Fig. 3g)34.”
From Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I (2013) · cites this paper as [34]
Modeling using prokaryotic complex I structures produced an orthologous mammalian core structure containing ND3 Cys39.
“We modeled the location of ND3 Cys39 using structures of prokaryotic complex I (refs. 32–34). This modeling led to an orthologous mammalian core structure containing ND3 Cys39 (Fig. 3f,g and Supplementary Figs. 14 and 15).”
From Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex I (2013) · cites this paper as [34]
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- Authors
- Baradaran, R., Berrisford, J. M., Minhas, G. S., & Sazanov, L. A.
- Affiliations
- MRC Mitochondrial Biology Unit (GB)
- European Bioinformatics Institute (GB)
- Corresponding author
- Sazanov, Leonid A.
- Venue
- Nature
- Published
- 2013-02
- Volume
- 494
- Issue
- 7438
- Pages
- 443-448
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3672946
- OpenAlex
- W2058570690
- Cited by
- 797
- References
- 58
- Citations by year
- 2026: 38 · 2025: 31 · 2024: 33 · 2023: 40 · 2022: 62 · 2021: 58 · 2020: 65 · 2019: 52 · 2018: 73 · 2017: 60 · 2016: 82 · 2015: 67 · 2014: 83 · 2013: 50 · 2012: 2
- FWCI
- 42.39
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DORA PSI (Paul Scherrer Institute) (submittedVersion)
- Funders
- European Synchrotron Radiation Facility
- Medical Research Council
- Topics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- mitochondrial complex I, mitochondrial electron transport chain, Thermus thermophilus, quinone binding site, proton translocation, iron-sulfur clusters, ND1, conformational coupling, neurodegenerative diseases
- MeSH terms
- Cell Membrane, Humans, Models, Molecular, NAD, Oxidation-Reduction, Protons, Ubiquinone, Benzoquinones, Thermus thermophilus, Protein Folding, Crystallography, X-Ray, Proton-Motive Force, Protein Subunits, Electron Transport Complex I, Hydrophobic and Hydrophilic Interactions
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