Structure and mechanism of tryptophylquinone enzymes
1Department of Biochemistry, The University of Mississippi Medical Center, 2500 N. State St., Jackson, MS 39216-4505, USA. vdavidson@biochem.umsmed.edu
Abstract:
Tryptophylquinone cofactors are formed by posttranslational modifications that result in the incorporation of two oxygens into a tryptophan side chain, and the covalent cross-linking of that side chain to another amino acid residue. Tryptophylquinone enzymes catalyze the oxidative deamination of primary amines, and utilize other redox proteins as electron acceptors. Mechanistic and structural studies of these enzymes are providing insight into how these enzymes utilize these highly reactive protein-derived quinones in a controlled manner to facilitate biologically important catalytic and electron transfer reactions.
Related Concept Videos
Oxidation of Phenols to Quinones
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox property is crucial in...
ATP Synthase: Mechanism
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
Electron Transport Chain: Complex III and IV
ATP Synthase: Structure
Repressible Operon: trp Operon


