|Title||Organization of iron-sulfur clusters in respiratory complex I.|
|Publication Type||Journal Article|
|Year of Publication||2005|
|Authors||Hinchliffe, P, Sazanov, LA|
|Date Published||2005 Jul 29|
|Keywords||Binding Sites, Catalytic Domain, Crystallography, X-Ray, Electron Spin Resonance Spectroscopy, Electron Transport, Electron Transport Complex I, Flavin Mononucleotide, Iron, Models, Molecular, NAD, Oxidation-Reduction, Protein Structure, Quaternary, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Subunits, Sulfur, Thermus thermophilus|
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.