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  • Title: Photoaffinity labeling of a mitochondrial hydrophobic protein by an anisotropic inhibitor of energy transduction in oxidative phosphorylation.
    Author: Higuti T, Ohe T, Arakaki N, Kotera Y.
    Journal: J Biol Chem; 1981 Oct 10; 256(19):9855-60. PubMed ID: 7275983.
    Abstract:
    The monoazide derivative of ethidium, the parent compound of which is an anisotropic inhibitor of energy transduction in oxidative phosphorylation, was synthesized and shown to be useful as a photoaffinity probe. Results showed that monoazide ethidium specifically binds to a hydrophobic protein of mitochondria (with an apparent molecular weight of about 6200 in the presence of 0.1% sodium dodecyl sulfate). The molar binding ratios of monoazide ethidium to protein were about 5 and 17 with protein in the nonenergized and energized states, respectively. This protein differed from the dicyclohexylcarbodiimide-binding protein. We refer to this new hydrophobic protein, anisotropic inhibitor-binding protein, in this paper.
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