Structural and functional insights into sulfide:quinone oxidoreductase

Biochemistry. 2009 Jun 23;48(24):5613-22. doi: 10.1021/bi9003827.


A sulfide:quinone oxidoreductase (SQR) was isolated from the membranes of the hyperthermoacidophilic archaeon Acidianus ambivalens, and its X-ray structure, the first reported for an SQR, was determined to 2.6 A resolution. This enzyme was functionally and structurally characterized and was shown to have two redox active sites: a covalently bound FAD and an adjacent pair of cysteine residues. Most interestingly, the X-ray structure revealed the presence of a chain of three sulfur atoms bridging those two cysteine residues. The possible implications of this observation in the catalytic mechanism for sulfide oxidation are discussed, and the role of SQR in the sulfur dependent bioenergetics of A. ambivalens, linked to oxygen reduction, is addressed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acidianus / enzymology
  • Acidianus / metabolism
  • Amino Acid Sequence
  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / metabolism
  • Catalytic Domain
  • Crystallography, X-Ray
  • Cysteine / genetics
  • Cysteine / metabolism
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism
  • Molecular Weight
  • Oxidation-Reduction
  • Quinone Reductases / chemistry*
  • Quinone Reductases / metabolism
  • Structure-Activity Relationship
  • Sulfides / chemistry
  • Sulfides / metabolism


  • Archaeal Proteins
  • Membrane Proteins
  • Sulfides
  • Quinone Reductases
  • sulfide quinone reductase
  • Cysteine

Associated data

  • PDB/3H8I
  • PDB/3H8L