Mechanistic studies on phenylalanine hydroxylase from Chromobacterium violaceum. Evidence for the formation of an enzyme-oxygen complex

Citations Over TimeTop 19% of 1989 papers

Abstract

Steady-state kinetic analysis of pterin-dependent phenylalanine hydroxylase from Chromobacterium violaceum indicated that the enzyme follows a partially ordered reaction mechanism. The data suggested that oxygen is the first substrate to bind to the enzyme. This result was further supported by rapid-quench experiments in which the enzyme-oxygen complex was trapped to yield product. Additional support for the presence of an enzyme-oxygen complex was derived from magnetic susceptibility measurements of molecular oxygen in the presence and absence of cuprous phenylalanine hydroxylase. The magnetic susceptibility of dissolved oxygen decreased in the presence of the enzyme, supporting a direct oxygen-metal interaction.

Related Papers

• → Regulation of rat liver phenylalanine hydroxylase. III. Control of catalysis by (6R)-tetrahydrobiopterin and phenylalanine.(1994)59 cited
• → Spectroscopic and Kinetic Studies of PKU−Inducing Mutants of Phenylalanine Hydroxylase: Arg158Gln and Glu280Lys(2003)31 cited
• → Delineation of the catalytic core of phenylalanine hydroxylase and identification of glutamate 286 as a critical residue for pterin function.(1994)49 cited
• → Copper-Pteridine Chemistry. Structures, Properties, and Phenylalanine Hydroxylase Models(1993)5 cited
• → Spectroscopic Characterization of Human Liver Pterin 4a-Carbinolamine Dehydratase(1993)4 cited