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• W2110176312 abstract "Ubiquinone-2 (UQ-2) selectively labeled with 13C (I =1/2) at either the position 1- or the 4-carbonyl carbon is incorporated into the ubiquinol oxidase bo3 from Escherichia coli in which the native quinone (UQ-8) has been previously removed. The resulting stabilized anion radical in the high-affinity quinone-binding site (QH•-) is investigated using multifrequency (9, 34, and 94 GHz) electron paramagnetic resonance (EPR) spectroscopy. The corresponding spectra reveal dramatic differences in 13C hyperfine couplings indicating a strongly asymmetric spin density distribution over the quinone headgroup. By comparison with previous results on labeled ubisemiquinones in proteins as well as in organic solvents, it is concluded that QH•- is most probably bound to the protein via a one-sided hydrogen bond or a strongly asymmetric hydrogen-bonding network. This observation is discussed with regard to the function of QH in the enzyme and contrasted with the information available on other protein-bound semiquinone radicals." @default.
• W2110176312 created "2016-06-24" @default.
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• W2110176312 date "2003-04-24" @default.
• W2110176312 modified "2023-10-16" @default.
• W2110176312 title "Asymmetric Binding of the High-Affinity Q_H^•^- Ubisemiquinone in Quinol Oxidase (<i>bo</i>₃) from <i>Escherichia coli</i> Studied by Multifrequency Electron Paramagnetic Resonance Spectroscopy" @default.
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• W2110176312 doi "https://doi.org/10.1021/bi034010z" @default.
• W2110176312 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12741819" @default.
• W2110176312 hasPublicationYear "2003" @default.
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