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Updated: Jul 17, 2026

Detection of Invasive Pulmonary Aspergillosis in Haematological Malignancy Patients by using Lateral-flow Technology
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Identification of the BAL-labile factor.

E C Slater, S de Vries

    Nature
    |December 25, 1980
    PubMed
    Summary

    Researchers identified a key factor in cellular respiration. This iron-sulphur protein, crucial for electron transfer between cytochromes b and c, is inactivated by 2,3-dimercaptopropanol (BAL).

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    Area of Science:

    • Biochemistry
    • Cellular Respiration
    • Mitochondrial Function

    Background:

    • Previous studies showed 2,3-dimercaptopropanol (BAL) inactivates the succinate oxidase system in heart muscle preparations.
    • This inactivation occurs between cytochromes b and c and requires BAL oxidation.
    • The BAL-labile factor is also essential for NADH oxidation and is not cytochrome c1, myoglobin, or the antimycin-binding site.

    Purpose of the Study:

    • To identify the BAL-labile factor involved in electron transfer between cytochromes b and c.
    • To elucidate the role of this factor in the respiratory chain.

    Main Methods:

    • Biochemical assays on Keilin and Hartree heart-muscle preparation.
    • Spectroscopic studies to pinpoint the site of enzyme inactivation.
    • Comparison with known respiratory chain components.

    Main Results:

    • The BAL-labile factor is identical to the iron-sulphur protein identified by Rieske.
    • This protein is located in the central portion of the respiratory chain.
    • The iron-sulphur protein mediates electron transfer from cytochrome b to cytochrome c.

    Conclusions:

    • The Rieske iron-sulphur protein is the BAL-labile factor responsible for electron transfer between cytochromes b and c.
    • This finding clarifies a critical step in mitochondrial respiration and NADH oxidation.

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