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Related Experiment Videos

Catalysis in fumarate reductase.

G A Reid1, C S Miles, R K Moysey

  • 1Institute of Cell and Molecular Biology, University of Edinburgh, UK. graeme.reid@ed.ac.uk

Biochimica Et Biophysica Acta
|September 27, 2000
PubMed
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Shewanella bacteria use a unique soluble enzyme for fumarate reduction, a key anaerobic respiration process. Structural and mutation studies reveal an arginine residue is crucial for catalysis, unlike histidine.

Area of Science:

  • Microbiology
  • Biochemistry
  • Structural Biology

Background:

  • Many bacteria respire anaerobically using fumarate as a terminal electron acceptor.
  • Fumarate reductases are typically membrane-bound, but Shewanella species utilize a soluble, periplasmic flavocytochrome c(3).

Purpose of the Study:

  • To elucidate the structural basis and catalytic mechanism of the soluble fumarate reductase from Shewanella species.
  • To identify the specific amino acid residues involved in substrate binding and catalysis.

Main Methods:

  • X-ray crystallography to determine the structures of fumarate reductases from two Shewanella species.
  • Site-directed mutagenesis to investigate the role of specific amino acid residues in enzyme activity.

Main Results:

Related Experiment Videos

  • Structures revealed conserved active sites with fumarate, succinate, and hydrated fumarate ligands bound near the FAD cofactor.
  • Identified key residues for substrate binding and catalysis.
  • Mutational analysis demonstrated that an arginine residue (Arg402) is essential for catalysis, while active site histidines are not.

Conclusions:

  • The soluble fumarate reductase from Shewanella shares conserved active site features with other fumarate reductases.
  • An arginine residue acts as the proton donor in the fumarate to succinate conversion, clarifying a long-standing question in the enzyme's mechanism.