Chloroperoxidase-catalyzed oxidation of N-methyl-4-chloroaniline
Chloroperoxidase catalyzed the H2O2 oxidative conversion of N-methyl-4-chloroaniline to 4-chloronitrosobenzene, 4-chloroaniline and a mixture of complex products.
Chloroperoxidase. I. Isolation and properties of the crystalline glycoprotein.
Abstract Chloroperoxidase from Caldariomyces fumago has been isolated in crystalline form. The prosthetic group of chloroperoxidase is ferriprotoporphyrin IX. On the basis of the heme content, the minimal molecular weight of chloroperoxidase is 40,200. On the basis of hydrodynamic measurements, the molecular weight of chloroperoxidase is approximately 42,000. Therefore, in solution at neutral pH, chloroperoxidase behaves as a monomeric species. The spectral properties of the oxidized and reduced forms of the enzyme and also of the azide and cyanide complexes are reported. The amino acid composition of chloroperoxidase is reported. Chloroperoxidase is rich in aspartic acid, glutamic acid, and serine and proline residues. These four amino acids constitute 45% of the total amino acid content. Chloroperoxidase is a glycoprotein. Approximately 25 to 30% of the molecule is carbohydrate. Chromatography of acid hydrolysates reveals that glucosamine and arabinose are major constituents.
Interaction of Diclofop-Methyl and MCPA on Wild Oats (Avena fatua)
Diclofop-methyl {methyl 2-[4-(2,4-dichlorophenoxy)phenoxy] propanoate} loses part of its activity on wild oats (Avena fatua L.) when it is applied in combination with ester or amine formulations of MCPA {[4-chloro-o-tolyl)oxy] acetic acid.} Uptake of diclofop-methyl is reduced in the presence of commercial formulations of MCPA, particularly amine formulations, which are only partly compatible with the diclofop-methyl formulation. With added MCPA, regardless of formulation, hydrolysis of diclofop-methyl to the acid diclofop is slowed down, both in intact wild oat plants and in a crude leaf extract. At the same time, conversion of any acid formed to inactive conjugates is accelerated in the presence of MCPA. It is concluded that the loss of activity of diclofop-methyl by MCPA can be accounted for by the effects of MCPA on uptake and metabolic conversion of diclofop-methyl.