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Structure of the Hydrophilic Domain of Respiratory Complex I from <i>Thermus thermophilus</i>
49/49 checkable references clean · checked 2026-07-22
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
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The 49 checked references that resolve
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The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains
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The Proton-Translocating NADH−Quinone Oxidoreductase in the Respiratory Chain: The Secret Unlocked
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Analysis of the Subunit Composition of Complex I from Bovine Heart Mitochondria*S
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Three-dimensional structure of bovine NADH:ubiquinone oxidoreductase (complex I) at 22 å in ice
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Isolation, Characterization and Electron Microscopic Single Particle Analysis of the NADH:Ubiquinone Oxidoreductase (Complex I) from the Hyperthermophilic Eubacterium<i>Aquifex aeolicus</i>
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Consistent structure between bacterial and mitochondrial NADH:ubiquinone oxidoreductase (complex I)
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Resolution of NADH:ubiquinone oxidoreductase from bovine heart mitochondria into two subcomplexes, one of which contains the redox centers of the enzyme
resolves10.1074/jbc.M308247200
The Location of NuoL and NuoM Subunits in the Membrane Domain of the Escherichia coli Complex I
resolves10.1016/S0014-5793(00)01867-6
The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane‐bound multisubunit hydrogenases
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Isolation and Characterization of the Proton-translocating NADH:ubiquinone Oxidoreductase from Escherichia coli
resolves10.1074/jbc.M410377200
Characterization of the Iron-Sulfur Cluster N7 (N1c) in the Subunit NuoG of the Proton-translocating NADH-quinone Oxidoreductase from Escherichia coli
resolves10.1038/46972
Natural engineering principles of electron tunnelling in biological oxidation–reduction
resolves10.1107/S0907444904026460
Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
resolves10.1016/S0022-2836(05)80134-2
SCOP: A structural classification of proteins database for the investigation of sequences and structures
resolves10.1006/jmbi.2000.3871
Structure of a thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus
resolves10.1038/nsb969
Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A
resolves10.1073/pnas.042664399
Structure of adenylylsulfate reductase from the hyperthermophilic
<i>Archaeoglobus fulgidus</i>
at 1.6-Å resolution
resolves10.1126/science.282.5395.1853
X-ray Crystal Structure of the Fe-Only Hydrogenase (CpI) from Clostridium pasteurianum to 1.8&nbsp;Angstrom Resolution
resolves10.1074/jbc.M212275200
Characterization of Cluster N5 as a Fast-relaxing [4Fe-4S] Cluster in the Nqo3 Subunit of the Proton-translocating NADH-ubiquinone Oxidoreductase from Paracoccus denitrificans
resolves10.1021/bi049938l
The Catalytic Subunit of <i>Escherichia coli</i> Nitrate Reductase A Contains a Novel [4Fe-4S] Cluster with a High-Spin Ground State<sup>,</sup>
resolves10.1016/S0969-2126(99)80010-0
Crystal structure of the first dissimilatory nitrate reductase at 1.9 Å solved by MAD methods
resolves10.1016/S0005-2728(98)00022-X
Organization and evolution of structural elements within complex I
resolves10.1074/jbc.273.41.26349
Structural Analysis of the fds Operon Encoding the NAD+-linked Formate Dehydrogenase of Ralstonia eutropha
resolves10.1016/j.bbabio.2003.09.001
The mitochondrial and prokaryotic proton-translocating NADH:ubiquinone oxidoreductases: similarities and dissimilarities of the quinone-junction sites
resolves10.1074/jbc.M308967200
Iron-Sulfur Cluster N2 of the Escherichia coli NADH:Ubiquinone Oxidoreductase (Complex I) Is Located on Subunit NuoB
resolves10.1074/jbc.M102296200
A Central Functional Role for the 49-kDa Subunit within the Catalytic Core of Mitochondrial Complex I
resolves10.1021/bi048132i
Characterization of the Δμ<sub>H</sub><sup><sub>+</sub></sup>-Sensitive Ubisemiquinone Species (SQ<sub>Nf</sub>) and the Interaction with Cluster N2: New Insight into the Energy-Coupled Electron Transfer in Complex I
resolves10.1016/S0014-5793(98)00719-4
The 49‐kDa subunit of NADH‐ubiquinone oxidoreductase (Complex I) is involved in the binding of piericidin and rotenone, two quinone‐related inhibitors
resolves10.1074/jbc.M313180200
Functional Significance of Conserved Histidines and Arginines in the 49-kDa Subunit of Mitochondrial Complex I
resolves10.1073/pnas.160270897
Crystal structure of
<i>Escherichia coli</i>
CyaY protein reveals a previously unidentified fold for the evolutionarily conserved frataxin family
resolves10.1126/science.1098991
Frataxin Acts as an Iron Chaperone Protein to Modulate Mitochondrial Aconitase Activity
resolves10.1074/jbc.C400107200
Frataxin-mediated Iron Delivery to Ferrochelatase in the Final Step of Heme Biosynthesis
resolves10.1021/bi00199a034
Thermodynamic Analysis of Flavin in Mitochondrial NADH:Ubiquinone Oxidoreductase (Complex I)
resolves10.1016/0014-5793(90)80753-6
Coupling site I and the rotenone‐sensitive ubisemiquinone in tightly coupled submitochondrial particles
resolves10.1074/jbc.M310341200
Characterization of Superoxide-producing Sites in Isolated Brain Mitochondria
resolves10.1074/jbc.M503936200
Superoxide Generation from Mitochondrial NADH Dehydrogenase Induces Self-inactivation with Specific Protein Radical Formation
resolves10.1023/A:1010722717257
Complex I: A Chimaera of a Redox and Conformation-Driven Proton Pump?
resolves10.1021/bi00181a018
Catalytic Sector of Complex I (NADH:Ubiquinone Oxidoreductase):Subunit Stoichiometry and Substrate-Induced Conformation Changes
resolves10.1021/ja961465l
Novel Redox Chemistry of [3Fe−4S] Clusters: Electrochemical Characterization of the All-Fe(II) Form of the [3Fe−4S] Cluster Generated Reversibly in Various Proteins and Its Spectroscopic Investigation in <i>Sulfolobus acidocaldarius</i> Ferredoxin
The 4 references without a DOI — listed, not checked
no DOI — not checkedP. Hinchliffe J. Carroll L. A. Sazanov in preparation.
no DOI — not checkedMaterials and methods are available as supporting material on Science Online.
no DOI — not checkedD. J. Morgan L. A. Sazanov unpublished data.
no DOI — not checkedThis work was funded by the Medical Research Council. We thank J. E. Walker A. G. W. Leslie and A. G. Murzin for helpful discussions of the manuscript; the European Synchrotron Radiation Facility for provision of synchrotron radiation facilities; and the staff of beamlines ID23 and ID29 for assistance. The coordinates and the structure factors have been deposited in the Protein Data Bank (accession code 2FUG).
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