Organization of iron-sulfur clusters in respiratory complex I.

TitleOrganization of iron-sulfur clusters in respiratory complex I.
Publication TypeJournal Article
Year of Publication2005
AuthorsHinchliffe, P, Sazanov, LA
Date Published2005 Jul 29
KeywordsBinding 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.

Alternate JournalScience
Citation Key10.1126/science.1113988
PubMed ID16051796