A molecular orbital study on the interaction between the cytochrome P-450 and its substrates.

Models for the interaction of the cytochrome P-450 with its substrates, namely for the type I interaction are proposed in which the molecular planes of the aromatic substrate and the porphyrins of P-450 are in parallel. Optical values such as transition energies and oscillator strengths for the isolated P-450 and P-450-substrate complex are calculated by means of molecular orbital method (ASMO SCF CI method), and they are compared with the observed values. The fact that no appreciable shift in the absorption peak of Soret band of P-450 was observed upon addition of substrate is reflected well in the calculation. Similarly, the well-known fact that the absorbance of the P-450 was decreased by mixing it with the substrate is also explained well by the calculated oscillator strength for the isolated P-450 and the stacked complexes. From the good agreement between the calculated results and the observed ones, it is suggested that the proposed models might be true reflections of the interactions between the P-450 and its substrates.     

D-amino acid oxidase in mouse liver

1. An appreciable amount of D-amino acid oxidase was found in the extract of mouse liver by enzyme-linked immunosorbent assay (ELISA). 2. The content of the enzyme in the kidney and heart extracts was also measured by the assay.