Oxidoreduction properties of bound ubiquinone in Complex I from Escherichia coli.

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 (<-300mV) was found for the bound ubiquinone, more than 400mV 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.