Verkhovskaya 2014 Biochim Biophys Acta
| Verkhovskaya M, Wikström M (2014) Oxidoreduction properties of bound ubiquinone in Complex I from Escherichia coli. Biochim Biophys Acta 1837:246-50. https://doi.org/10.1016/j.bbabio.2013.11.001 |
Verkhovskaya M, Wikstroem Marten KF (2014) Biochim Biophys Acta
Abstract: The exploration of the redox chemistry of bound ubiquinone during catalysis is a prerequisite for the understanding of the mechanism by which Complex I (nicotinamide adenine dinucleotide (NADH):ubiquinone oxidoreductase) transduces redox energy into an electrochemical proton gradient. Studies of redox dependent changes in the spectrum of Complex I from Escherichia coli in the mid- and near-ultraviolet (UV) and visible areas were performed to identify the spectral contribution, and to determine the redox properties, of the tightly bound ubiquinone. A very low midpoint redox potential (<-300 mV) was found for the bound ubiquinone, more than 400 mV lower than when dissolved in a phospholipid membrane. This thermodynamic property of bound ubiquinone has important implications for the mechanism by which Complex I catalyzes proton translocation.
• Bioblast editor: Gnaiger E
Labels:
Preparation: Enzyme
Enzyme: Complex I
