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Related Experiment Videos

Complex II from a structural perspective.

Rob Horsefield1, So Iwata, Bernadette Byrne

  • 1Department of Biological Sciences, Imperial College London, SW7 2AZ, UK. b.byrne@imperial.ac.uk

Current Protein & Peptide Science
|April 14, 2004
PubMed
Summary
This summary is machine-generated.

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The structure of succinate:quinone oxidoreductase (SQR) from E. coli reveals its molecular design and electron transport pathway. This finding advances understanding of SQR

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Succinate:quinone oxidoreductase (SQR) links the Krebs cycle to the aerobic respiratory chain.
  • Previous structure-function insights relied on homologous quinol:fumarate reductase (QFR).

Purpose of the Study:

  • To present the structure of SQR from Escherichia coli.
  • To elucidate SQR's molecular design, mechanism, and electron transport pathway.
  • To compare SQR with QFR and related flavoproteins.

Main Methods:

  • X-ray crystallography of SQR from E. coli.
  • Comparative structural analysis.

Main Results:

  • The E. coli SQR structure reveals its molecular architecture and electron transport pathway.

Related Experiment Videos

  • Common amino acid residues facilitate succinate-fumarate inter-conversion.
  • Structural insights explain the co-occurrence of SQR and QFR in some organisms.

    • Conclusions:

    • The E. coli SQR structure provides critical insights into its function and mechanism.
    • Structural comparisons highlight conserved features in related flavoproteins.
    • This work advances the understanding of the Complex II superfamily.