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- W2025495821 abstract "The technique of distance measurement utilizing spin relaxation enhancement by an external probe has been extended to the study of intrinsic semiquinone radicals through the use of holmium-EDTA complexes and continuous wave electron paramagnetic resonance spectroscopy. This technique has been used to determine the distance of the semiquinone anion. Q1 (also designate as Qn− or Qc−), from the surface of the ubiquinone cytochrome c oxidoreductase, consisting of only three subunits, in membrane particles from Rhodobacter capsulates. The location of the semiquinone anion is 6–10Åfrom the N side protein, establishing that there are two separate quinone reaction sites, i.e., ‘Q1’ and ‘Q0’, within this complex on opposite sides of the membrane. The results are discussed in relation to reported ENDOR, EPR, and optical studies of the mitochondrial counterpart." @default.
- W2025495821 created "2016-06-24" @default.
- W2025495821 creator A5007595238 @default.
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- W2025495821 date "1992-04-01" @default.
- W2025495821 modified "2023-09-25" @default.
- W2025495821 title "Determination of the position of the Qi− quinone binding from the protein surface of the cytochrome bc1 complex in Rhodobacter capsulates chromatophores" @default.
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- W2025495821 doi "https://doi.org/10.1016/0005-2728(92)90127-n" @default.
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