[Geometry of the complexes between horseradish peroxidase and aromatic substrates].

Geometry of the complexes between horse radish peroxidase and aromatic substrates was studied by means of new technique of precision measurement of NMR shifts. Weak dipolar shifts of hydroquinone and parametoxiphenole PMR in the presence of high spin peroxidase were recorded. Polar and azimuth angles in coordinate axes of peroxidase hem for the binding site on the enzyme of the aromatic part of the substrate molecule were estimated for the first time.