Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus

@article{Sazanov2006StructureOT,
  title={Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus},
  author={Leonid A. Sazanov and Philip Hinchliffe},
  journal={Science},
  year={2006},
  volume={311},
  pages={1430 - 1436}
}
Respiratory complex I plays a central role in cellular energy production in bacteria and mitochondria. Its dysfunction is implicated in many human neurodegenerative diseases, as well as in aging. The crystal structure of the hydrophilic domain (peripheral arm) of complex I from Thermus thermophilus has been solved at 3.3 angstrom resolution. This subcomplex consists of eight subunits and contains all the redox centers of the enzyme, including nine iron-sulfur clusters. The primary electron… Expand
Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus
TLDR
Complex I (NADH:ubiquinone oxidoreductase) plays a central role in cellular energy production, coupling electron transfer between NADH and quinone to proton translocation and the structure of the complete enzyme and the coupling mechanism are not yet known. Expand
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
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 bacterial respiratory complex I.
TLDR
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TLDR
The architecture of the complex provides strong clues about the coupling mechanism: the conformational changes at the interface of the two main domains may drive the long amphipathic α-helix of NuoL in a piston-like motion, tilting nearby discontinuous TM helices, resulting in proton translocation. Expand
Structure of Complex I
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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
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 Respiratory Complex I
TLDR
Structures of the reduced hydrophilic domain revealed how NADH interacts with the enzyme and provided clues about the coupling mechanism, and the arrangement of redox centers, including nine iron–sulfur clusters. Expand
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