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Related Experiment Videos

Mitochondrial rhodanese: membrane-bound and complexed activity.

K Ogata1, M Volini

  • 1Department of Biochemistry and Biophysics, John A. Burns School of Medicine, University of Hawaii, Honolulu 96822.

The Journal of Biological Chemistry
|May 15, 1990
PubMed
Summary

Mitochondrial rhodanese, a sulfurtransferase, is partly membrane-bound and forms iron-sulfur centers. This complex modulates mitochondrial respiration rates, supporting its role in cellular energy production.

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Area of Science:

  • Biochemistry
  • Mitochondrial Biology
  • Enzymology

Background:

  • Rhodanese (sulfurtransferase) exists in phosphorylated and dephosphorylated forms.
  • These forms are proposed to interact with membrane-bound iron-sulfur centers.
  • This interaction is hypothesized to modulate mitochondrial respiration.

Purpose of the Study:

  • To investigate the structural aspects of the mitochondrial rhodanese system.
  • To determine the localization and interactions of rhodanese within mitochondria.
  • To further elucidate rhodanese's role in mitochondrial respiration.

Main Methods:

  • Sequential extraction of lysed mitochondria using phosphate buffer and cholate.
  • Gel filtration chromatography (Sephadex G-100) to resolve protein complexes.

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  • In vitro assays to assess iron-sulfur center formation and enzyme activity.

    • Main Results:

    • Approximately 30% of bovine liver rhodanese activity is membrane-bound.
    • Bound rhodanese exists in complexes with other mitochondrial proteins.
    • The rhodanese-containing complex facilitates iron-sulfur center formation in the presence of thiosulfate, iron, and a reducing agent.
    • Similar results were observed with rat liver mitochondria.

    Conclusions:

    • Liver rhodanese is partially bound to the mitochondrial membrane as part of a multiprotein complex.
    • This complex is involved in the formation of iron-sulfur centers.
    • The findings support the proposed role of rhodanese in modulating mitochondrial respiratory activity.