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Related Experiment Videos

Disulfide bonds are generated by quinone reduction.

M W Bader1, T Xie, C A Yu

  • 1Department of Biology, University of Michigan, Ann Arbor, Michigan 48109-1048, USA.

The Journal of Biological Chemistry
|June 16, 2000
PubMed
Summary
This summary is machine-generated.

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The DsbB protein generates new disulfide bonds using quinones, a novel catalytic activity. This system is essential for oxidative folding and protein maturation in vivo.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Disulfide bond formation is crucial for protein folding and function.
  • The origin of disulfide bonds in vivo remains largely unknown.
  • Existing knowledge focuses on disulfide exchange, not de novo bond generation.

Purpose of the Study:

  • To investigate the de novo origin of disulfide bonds.
  • To characterize the enzymatic activity of DsbB in disulfide bond formation.
  • To elucidate the role of quinones in disulfide bond generation.

Main Methods:

  • Development of a novel assay to study disulfide bond formation.
  • In vitro reconstitution of oxidative folding using DsbA, DsbB, and quinones.
  • Characterization of quinone reduction during the reaction.

Related Experiment Videos

  • Assessment of ribonuclease A refolding and DsbC requirement.

    • Main Results:

    • DsbB utilizes quinones to generate disulfide bonds de novo.
    • This DsbB-quinone activity is identified as a major source of disulfides in vivo.
    • The DsbA-DsbB-quinone system catalyzes oxidative refolding of ribonuclease A.
    • DsbC is required for regaining ribonuclease activity, indicating non-native disulfide bonds.

    Conclusions:

    • DsbB possesses a novel catalytic activity involving quinone reduction for disulfide bond generation.
    • The DsbA-DsbB-quinone system is essential for oxidative folding in vivo.
    • Kinetic isolation of oxidative and isomerase pathways prevents cellular oxidative damage.