In
A. aeolicus, SQR is an
integral monotopic protein, so it penetrates into the hydrophobic region of the plasma membrane. The SQR reaction takes place in two half reactions, sulfide oxidation and quinone reduction. The active site of SQR is composed of a region that interacts with the periplasmic space and sulfide connected by a FAD cofactor and a trisulfide bridge to a quinone. FAD receives two electrons from sulfide and transfers the electrons one at time to the quinone. The amino acids surrounding the quinone are all hydrophobic. Also, there is a highly conserved region of uncharged amino acids, phenylalanine and isoleucine, that surround the benzene ring of the quinone. SQR is a member of the
flavoprotein disulfide reductase (FDR) superfamily. FDRs are typically characterized as being dimeric or two subunit proteins, but sulfide quinone oxidoreductase is a trimeric protein. The main purpose of SQR is to detoxify
sulfide. Sulfide is a toxic chemical that inhibits enzymatic reactions, especially those with metal cofactors. Most notably, sulfide inhibits cytochrome oxidase found in the electron transport chain. SQR oxidizes sulfide and produces non-toxic products. == Role in metabolism ==