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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Verkhovsky, Michael Bloch, Dmitry A. Verkhovskaya, Marina |
| Description | Author Affiliation: Verkhovsky M ( University of Helsinki, Finland.) |
| Abstract | NADH:ubiquinone oxidoreductase (Complex I), the electron input enzyme in the respiratory chain of mitochondria and many bacteria, couples electron transport to proton translocation across the membrane. Complex I is a primary proton pump; although its proton translocation mechanism is yet to be known, it is considered radically different from any other mechanism known for redox-driven proton pumps: no redox centers have been found in its membrane domain where the proton translocation takes place. Here we studied the properties and the catalytic role of the enzyme-bound ubiquinone in the solubilized, purified Complex I from Escherichia coli . The ubiquinone content in the enzyme preparations was 1.3 ± 0.1 per bound FMN residue. Rapid mixing of Complex I with NADH, traced optically, demonstrated that both reduction and re-oxidation kinetics of ubiquinone coincide with the respective kinetics of the majority of Fe–S clusters, indicating kinetic competence of the detected ubiquinone. Optical spectroelectrochemical redox titration of Complex I followed at 270–280 nm, where the redox changes of ubiquinone contribute, did not reveal any transition within the redox potential range typical for the membrane pool, or loosely bound ubiquinone (ca. + 50–+ 100 mV vs. NHE, pH 6.8). The transition is likely to take place at much lower potentials ( $E_{m}$ ≤−200 mV). Such perturbed redox properties of ubiquinone indicate that it is tightly bound to the enzyme's hydrophobic core. The possibility of two ubiquinone-binding sites in Complex I is discussed. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 9 |
| Volume Number | 1817 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2012-09-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Electron Transport Complex I Metabolism Escherichia Coli Ubiquinone Binding Sites Electrochemistry Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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