PubMed Health⌕ Search

Biomedical subjects

P Mohr

Publications and source records attributed to P Mohr.

7 recordsLinked to original sources
PubMed1979

Comparison of the peroxidatic activity of cytochrome P-450 with other hemoproteins and model compounds.

The H2O2 dependent catalysis of cytochrome P-450 was compared with the catalytic mechanism of horse radish peroxidase, methemoglobin and iron protoporphyrin complexes. A relatively stable intermediate being comparable to compound I of horse radish peroxidase is formed in the case of iron porphyrin complexes, methemoglobin and probably cytochrome P-450. In the case of peroxidase compound II is the more stable intermediate. This could be the reason for the different catalytic properties of peroxidase on the one hand and iron porphyrin complexes, methemoglobin and cytochrome P-450 on the other hand.

Animals↗
PubMed1979

Electrochemical investigations on the oxygen activation by cytochrome P-450.

The application of cytochrome P-450 in substrate conversion is complicated both due to the limited stability and the cofactor regeneration problems. To overcome the disadvantages of NADPH consumption the transfer of the reduction equivalents from an electrode into the cytochrome P-450-system was studied: 1. NADPH was cathodically reduced at a mercury pool electrode. By immobilization of NADP on dialdehyde Sephadex the reductive recycling was possible. 2. Different forms of reduced oxygen were produced by the cathode: a) The reaction of O2- with deoxycorticosterone yields a carboxylic acid derivative. In contrast the cytochrome P-450 catalyzed NADPH-dependent reaction with the same substrate gives corticosterone, O2- represents only an intermediate in the activation of oxygen and is not the "activated oxygen" species. b) Molecular oxygen was reduced to HO2- and H2O2, respectively. The interaction of adsorbed cytochrome P-450 on the electrode surface with the reduced oxygen species in the absence of NADPH was studied. The electrochemically generated peroxide seems to be more active than added H2O2. 3. In a model of electro-enzyme-reactor several substrates were hydroxylated by microsomal cytochrome P-450 with cathodically reduced oxygen which substitutes NADPH.

Animals↗
PubMed1978

Aspects of application of cytochrome P-450 and related systems in substrate hydroxylation.

Extrapolating the recent progress in the near future the extensive utilization of cofactor-dependent enzymes (enzymes of the 3rd generation) for solving economic or medical problems will be restricted by the difficulties of cofactor regeneration. Real possibilities exist in analytical systems, for instance enzyme electrodes. In the present paper a special case of overcoming the cofactor regeneration in P-450 catalyzed substrate hydroxylation is demonstrated: The peroxide-dependent reaction gives the same products as obtained under physiological conditions; that is why in an electro-enzyme-reactor producing hydrogen peroxide by cathodic oxygen reduction a considerable simplification of the multi-enzyme complex is possible by omitting electron transfer proteins. At present the main problem is the instability of the terminal oxidase. Attempts are being made to solve these problems by immobilizing the protein or substituting P-450 by other hemoproteins or iron porphyrin derivatives.

Animals↗
PubMed1975

[Polarographic studies on the peroxidase activity of liganded deuterohemin].

The peroxidase activity of deuterohemin and deuterohemin complexes relative to the substrates pyrogallol and ascorbic acid was studied using d.c. polarography in aqueous solution. Imidazole and pyridine served as complex ligands. In the absence of the ligands, a continual rise in the substrate conversion rate with increasing H2O2 initial concentration is observed. Imidazole or pyridine were found to considerably increase the peroxidase activity of deuterohemin at low H2O2 concentrations. At high H2O2 concentrations, the dependence of the reaction rate on H2O2 concentration shows a bend, the reaction rate being in each case higher than that of free hemin under the same conditions. The reason of this fact is discussed to be a retarded formation of activated H2O2 hemin-ligand complexes at high H2O2 concentrations.

Deuteroporphyrins↗