Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.
Phire Hot Start DNA Polymerase

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Originally published in Science Express on 9 February 2006
Science 10 March 2006:
Vol. 311. no. 5766, pp. 1430 - 1436
DOI: 10.1126/science.1123809
Prev | Table of Contents | Next

Research Articles

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

Leonid A. Sazanov* and Philip Hinchliffe

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 acceptor, flavin-mononucleotide, is within electron transfer distance of cluster N3, leading to the main redox pathway, and of the distal cluster N1a, a possible antioxidant. The structure reveals new aspects of the mechanism and evolution of the enzyme. The terminal cluster N2 is coordinated, uniquely, by two consecutive cysteines. The novel subunit Nqo15 has a similar fold to the mitochondrial iron chaperone frataxin, and it may be involved in iron-sulfur cluster regeneration in the complex.

Medical Research Council Dunn Human Nutrition Unit, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 2XY, U.K.

* To whom correspondence should be addressed. E-mail: sazanov{at}mrc-dunn.cam.ac.uk

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Two Circular Chromosomes of Unequal Copy Number Make Up the Mitochondrial Genome of the Rotifer Brachionus plicatilis.
K. Suga, D. B. Mark Welch, Y. Tanaka, Y. Sakakura, and A. Hagiwara (2008)
Mol. Biol. Evol. 25, 1129-1137
   Abstract »    Full Text »    PDF »
Real-time electron transfer in respiratory complex I.
M. L. Verkhovskaya, N. Belevich, L. Euro, M. Wikstrom, and M. I. Verkhovsky (2008)
PNAS 105, 3763-3767
   Abstract »    Full Text »    PDF »
Characterization of the NuoM (ND4) Subunit in Escherichia coli NDH-1: CONSERVED CHARGED RESIDUES ESSENTIAL FOR ENERGY-COUPLED ACTIVITIES.
J. Torres-Bacete, E. Nakamaru-Ogiso, A. Matsuno-Yagi, and T. Yagi (2007)
J. Biol. Chem. 282, 36914-36922
   Abstract »    Full Text »    PDF »
Rows of ATP Synthase Dimers in Native Mitochondrial Inner Membranes.
N. Buzhynskyy, P. Sens, V. Prima, J. N. Sturgis, and S. Scheuring (2007)
Biophys. J. 93, 2870-2876
   Abstract »    Full Text »    PDF »
Exploring the Ubiquinone Binding Cavity of Respiratory Complex I.
M. A. Tocilescu, U. Fendel, K. Zwicker, S. Kerscher, and U. Brandt (2007)
J. Biol. Chem. 282, 29514-29520
   Abstract »    Full Text »    PDF »
Reevaluating the relationship between EPR spectra and enzyme structure for the iron sulfur clusters in NADH:quinone oxidoreductase.
G. Yakovlev, T. Reda, and J. Hirst (2007)
PNAS 104, 12720-12725
   Abstract »    Full Text »    PDF »
Analysis of the Assembly Profiles for Mitochondrial- and Nuclear-DNA-Encoded Subunits into Complex I.
M. Lazarou, M. McKenzie, A. Ohtake, D. R. Thorburn, and M. T. Ryan (2007)
Mol. Cell. Biol. 27, 4228-4237
   Abstract »    Full Text »    PDF »
Interaction of the Mitochondria-targeted Antioxidant MitoQ with Phospholipid Bilayers and Ubiquinone Oxidoreductases.
A. M. James, M. S. Sharpley, A.-R. B. Manas, F. E. Frerman, J. Hirst, R. A. J. Smith, and M. P. Murphy (2007)
J. Biol. Chem. 282, 14708-14718
   Abstract »    Full Text »    PDF »
Identification of Mitochondrial Complex I Assembly Intermediates by Tracing Tagged NDUFS3 Demonstrates the Entry Point of Mitochondrial Subunits.
R. O. Vogel, C. E. J. Dieteren, L. P. W. J. van den Heuvel, P. H. G. M. Willems, J. A. M. Smeitink, W. J. H. Koopman, and L. G. J. Nijtmans (2007)
J. Biol. Chem. 282, 7582-7590
   Abstract »    Full Text »    PDF »
Supramolecular Structure of the Mitochondrial Oxidative Phosphorylation System.
E. J. Boekema and H.-P. Braun (2007)
J. Biol. Chem. 282, 1-4
   Abstract »    Full Text »    PDF »
The Inhibition of Mitochondrial Complex I (NADH:Ubiquinone Oxidoreductase) by Zn2+.
M. S. Sharpley and J. Hirst (2006)
J. Biol. Chem. 281, 34803-34809
   Abstract »    Full Text »    PDF »
Structure of electron transfer flavoprotein-ubiquinone oxidoreductase and electron transfer to the mitochondrial ubiquinone pool.
J. Zhang, F. E. Frerman, and J.-J. P. Kim (2006)
PNAS 103, 16212-16217
   Abstract »    Full Text »    PDF »
Catalytic Importance of Acidic Amino Acids on Subunit NuoB of the Escherichia coli NADH:Ubiquinone Oxidoreductase (Complex I).
D. Flemming, P. Hellwig, S. Lepper, D. P. Kloer, and T. Friedrich (2006)
J. Biol. Chem. 281, 24781-24789
   Abstract »    Full Text »    PDF »
The Redox-Bohr Group Associated with Iron-Sulfur Cluster N2 of Complex I.
K. Zwicker, A. Galkin, S. Drose, L. Grgic, S. Kerscher, and U. Brandt (2006)
J. Biol. Chem. 281, 23013-23017
   Abstract »    Full Text »    PDF »
Mrs3p, Mrs4p, and Frataxin Provide Iron for Fe-S Cluster Synthesis in Mitochondria.
Y. Zhang, E. R. Lyver, S. A. B. Knight, D. Pain, E. Lesuisse, and A. Dancis (2006)
J. Biol. Chem. 281, 22493-22502
   Abstract »    Full Text »    PDF »
The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria.
L. Kussmaul and J. Hirst (2006)
PNAS 103, 7607-7612
   Abstract »    Full Text »    PDF »


ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)