[Absorption and magnetic circular dichroism spectra of nonequilibrium states of hemoproteins. III. Complexes of peroxidase].
Absorption and magnetic curcular dichroism spectra of nonequilibrium states of peroxidase  and its complexes with F-, N3-, CN- produced by reduction of oxidased forms of proteins by thermalysed electrons at 77 degrees K were studied. Mixtures of high spin and low spin ferroforms were found in nonequilibrium states of peroxidase and complexes with F- and N3-, the content of the high spin ferroform increasing as follows: N3- complex less than peroxidase less than fluorine complex. Only low spin ferroforms was found after low temperature reduction of the cyanide complex. The existence of the low spin ferroform in equilibrium states of peroxidase and its complex with F- was explained by location of iron near the porphyrine plane. In the case of azide and cyanide complexes the existence of the low spin form is due to the presence of these ligands in heme iron's coordination sphere. The temperature relaxation of all nonequilibrium forms was investigated and a possible mechanism of the process is proposed.
D001386:Azides; D002942:Circular Dichroism; D003486:Cyanides; D005459:Fluorides; D006420:Hemeproteins; D010084:Oxidation-Reduction; D010544:Peroxidases; D011485:Protein Binding; D011487:Protein Conformation; D013053:Spectrophotometry
D001386:Azides; D003486:Cyanides; D006420:Hemeproteins; D010544:Peroxidases; D005459:Fluorides
Spektry pogloshcheniia i magnitnogo krurovogo dikhroizma gemsoderzhashchikh belkov v neravnovesnykh sostoianiiakh. III. Kompleksy peroksidazy.