Interaction of complex I from Thermus thermophilus with quinone and quinone-like inhibitors

Quinone specificity of complex I.

This review considers the interaction of Complex I with different redox acceptors, mainly homologs and analogs of the physiological acceptor, hydrophobic Coenzyme Q. After examining the physical properties of the different quinones and their efficacy in restoring mitochondrial respiration, a survey ensues of the advantages and drawbacks of the quinones commonly used in Complex I activity determ...

Quinone binding and reduction by respiratory complex I.

Complex I (NADH:ubiquinone oxidoreductase) has a central function in oxidative phosphorylation and hence for efficient ATP production in most prokaryotic and eukaryotic cells. This huge membrane protein complex transfers electrons from NADH to ubiquinone and couples this exergonic redox reaction to endergonic proton pumping across bioenergetic membranes. Although quinone reduction seems to be c...

Binding sites of lipophilic quinone and quinone analogue inhibitors in the cytochrome b6f complex of oxygenic photosynthesis.

The main structural features of the cytochrome b6f complex, solved to 3.0-3.1 A (1 A = 10(-10) m) in the cyanobacterium Mastigocladus laminosus and the green alga Chlamydomonas reinhardtii are discussed. The discussion is focused on the binding sites of plastoquinone and quinone analogue inhibitors discerned in the structure. These sites mark the pathway(s) of quinone translocation across the c...

The Quinone Iron Acceptor Complex

Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus.

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 contai...