The architecture of respiratory complex I

@article{Efremov2010TheAO,
  title={The architecture of respiratory complex I},
  author={Rouslan G. Efremov and Rozbeh Baradaran and Leonid A. Sazanov},
  journal={Nature},
  year={2010},
  volume={465},
  pages={441-445}
}
Complex I is the first enzyme of the respiratory chain and has a central role in cellular energy production, coupling electron transfer between NADH and quinone to proton translocation by an unknown mechanism. Dysfunction of complex I has been implicated in many human neurodegenerative diseases. We have determined the structure of its hydrophilic domain previously. Here, we report the α-helical structure of the membrane domain of complex I from Escherichia coli at 3.9 Å resolution. The… Expand
Structure of the membrane domain of respiratory complex I
TLDR
The structure indicates that proton translocation in Esherichia coli complex I, uniquely, involves coordinated conformational changes in six symmetrical structural elements. Expand
Crystal structure of the entire respiratory complex I
TLDR
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. Expand
Structure of Complex I
Complex I is the first enzyme of the respiratory chain and plays a central role in cellular energy production. It has been implicated in many human neurodegenerative diseases, as well as in ageing.Expand
Structure of bacterial respiratory complex I.
TLDR
The crystal structures of the hydrophilic domain of complex I from Thermus thermophilus, the membrane domain from Escherichia coli and recently of the intact, entire complex I, which is the largest protein assembly of respiratory chains and one of the most elaborate redox membrane proteins known are solved. Expand
A long road towards the structure of respiratory complex I, a giant molecular proton pump.
TLDR
Determination of the structure of the entire complex was possible only through this step-by-step approach, building on from smaller subcomplexes towards the entire assembly, suggesting an unusual and unique coupling mechanism via long-range conformational changes. Expand
Structure and mechanism of respiratory complex I
NADH-ubiquinone oxidoreductase (complex I) is the first and largest enzyme in the respiratory chain of mitochondria and many bacteria. It couples electron transfer between NADH and ubiquinone to theExpand
Structure and mechanism of respiratory complex I, a giant molecular proton pump
NADH-ubiquinone oxidoreductase (complex I) is the first and largest enzyme in the respiratory chain of mitochondria and many bacteria. It couples electron transfer between NADH and ubiquinone to theExpand
Entire Respiratory Complex I from Thermus Thermophilus
TLDR
The atomic structure of the intact entire complex I from T. thermophilus is determined, and the redox energy of electron transfer is coupled to proton translocation by the mechanism proposed to involve long-range conformational changes. Expand
Essential regions in the membrane domain of bacterial complex I (NDH-1): the machinery for proton translocation
TLDR
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. Expand
Role of subunit NuoL for proton translocation by respiratory complex I.
The NADH:ubiquinone oxidoreductase, respiratory complex I, couples the transfer of electrons from NADH to ubiquinone with a translocation of protons across the membrane. The complex consists of aExpand
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References

SHOWING 1-10 OF 68 REFERENCES
Projection structure of the membrane domain of Escherichia coli respiratory complex I at 8 A resolution.
TLDR
Comparison of the projection map of negatively stained crystals with previously published low-resolution structures indicated that the characteristic curved shape of the membrane domain is remarkably well conserved between bacterial and mitochondrial enzymes, helping us to interpret projection maps in the context of the intact complex. Expand
Structural Basis for the Mechanism of Respiratory Complex I*
TLDR
Several x-ray structures of the oxidized and reduced hydrophilic domain of complex I from Thermus thermophilus are determined, suggesting a novel mechanism of coupling between electron transfer and proton translocation, combining conformational changes andProtonation/deprotonation of tandem cysteines. Expand
Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus
TLDR
The crystal structure of the hydrophilic domain (peripheral arm) of complex I from Thermus thermophilus has been solved at 3.3 angstrom resolution and reveals new aspects of the mechanism and evolution of the enzyme. Expand
Three-dimensional structure of respiratory complex I from Escherichia coli in ice in the presence of nucleotides.
TLDR
Observations indicate that conformational changes upon reduction with NADH, suggested to occur by a range of studies, are smaller than had been thought previously. Expand
Iron-sulfur clusters/semiquinones in complex I.
  • T. Ohnishi
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • 1998
TLDR
This mini-review describes three aspects of the recent progress in the study of the redox components of Complex I and suggests that the cluster N2 may have a unique ligand structure with an atypical cluster-ligation sequence motif located in the NuoB (NQO6/PSST) subunit rather than in the long advocated NuoI (NZO9/TYKY) subunits. Expand
Substrate-induced Conformational Change in Bacterial Complex I*
TLDR
Data indicate that upon NAD(P)H binding, the peripheral arm of the complex adopts a more open conformation, with increased distances between subunits, and the enzyme retains its L-shape in the presence of NADH, but exhibits a significantly more open or expanded structure both in the peripheral hand and in the membrane domain also. Expand
Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain.
TLDR
Novel mechanistic implications of the structure are discussed, and the effects of many known mutations of complex I subunits are interpreted in a structural context. Expand
Transmembrane orientation and topology of the NADH:quinone oxidoreductase putative quinone binding subunit NuoH.
TLDR
A topology model of NuoH is presented and four highly conserved hydrophilic sequence motifs facing the inside, bacterial cytoplasm are demonstrated, and implications from the model are discussed. Expand
Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I).
TLDR
It appears that the structural framework of procaryotic complex I is stabilized in eucaryotes by this additional mass, and a discrete location of additional protein in the peripheral arm of the mitochondrial complex is interpreted as being the possible position of two subunits with a specialized role in the biosynthesis of a yet unknown cofactor of complex I. Expand
Energy Converting NADH : Quinone Oxidoreductase ( Complex I )
NADH:quinone oxidoreductase (complex I) pumps protons across the inner membrane of mitochondria or the plasma membrane of many bacteria. Human complex I is involved in numerous pathologicalExpand
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1
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