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.

Science 29 July 2005:
Vol. 309. no. 5735, pp. 771 - 774
DOI: 10.1126/science.1113988
Prev | Table of Contents | Next

Reports

Organization of Iron-Sulfur Clusters in Respiratory Complex I

Philip Hinchliffe and Leonid A. Sazanov*

Complex I of respiratory chains plays a central role in bioenergetics and is implicated in many human neurodegenerative diseases. An understanding of its mechanism requires a knowledge of the organization of redox centers. The arrangement of iron-sulfur clusters in the hydrophilic domain of complex I from Thermus thermophilus has been determined with the use of x-ray crystallography. One binuclear and six tetranuclear clusters are arranged, maximally 14 angstroms apart, in an 84-angstrom-long electron transfer chain. The binuclear cluster N1a and the tetranuclear cluster N7 are not in this pathway. Cluster N1a may play a role in the prevention of oxidative damage. The structure provides a framework for the interpretation of the large amounts of data accumulated on complex I.

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

* 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:
Features of Subunit NuoM (ND4) in Escherichia coli NDH-1: TOPOLOGY AND IMPLICATION OF CONSERVED GLU144 FOR COUPLING SITE 1.
J. Torres-Bacete, P. K. Sinha, N. Castro-Guerrero, A. Matsuno-Yagi, and T. Yagi (2009)
J. Biol. Chem. 284, 33062-33069
   Abstract »    Full Text »    PDF »
Oxidative stress and disruption of labile iron generate specific auxotrophic requirements in Salmonella enterica.
M. P. Thorgersen and D. M. Downs (2009)
Microbiology 155, 295-304
   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 »
The mitochondrial energy transduction system and the aging process.
A. Navarro and A. Boveris (2007)
Am J Physiol Cell Physiol 292, C670-C686
   Abstract »    Full Text »    PDF »
Modeling mitochondrial function.
R. S. Balaban (2006)
Am J Physiol Cell Physiol 291, C1107-C1113
   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 »
ND3 and ND4L Subunits of Mitochondrial Complex I, Both Nucleus Encoded in Chlamydomonas reinhardtii, Are Required for Activity and Assembly of the Enzyme..
P. Cardol, M. Lapaille, P. Minet, F. Franck, R. F. Matagne, and C. Remacle (2006)
Eukaryot. Cell 5, 1460-1467
   Abstract »    Full Text »    PDF »
The MELAS mutations 3946 and 3949 perturb the critical structure in a conserved loop of the ND1 subunit of mitochondrial complex I.
M. Kervinen, R. Hinttala, H. M. Helander, S. Kurki, J. Uusimaa, M. Finel, K. Majamaa, and I. E. Hassinen (2006)
Hum. Mol. Genet. 15, 2543-2552
   Abstract »    Full Text »    PDF »
In Vivo Complementation of Complex I by the Yeast Ndi1 Enzyme: POSSIBLE APPLICATION FOR TREATMENT OF PARKINSON DISEASE.
B. B. Seo, E. Nakamaru-Ogiso, T. R. Flotte, A. Matsuno-Yagi, and T. Yagi (2006)
J. Biol. Chem. 281, 14250-14255
   Abstract »    Full Text »    PDF »
Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus.
L. A. Sazanov and P. Hinchliffe (2006)
Science 311, 1430-1436
   Abstract »    Full Text »    PDF »
Salmonella enterica Strains Lacking the Frataxin Homolog CyaY Show Defects in Fe-S Cluster Metabolism In Vivo.
E. Vivas, E. Skovran, and D. M. Downs (2006)
J. Bacteriol. 188, 1175-1179
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

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