The spin-state transition of the hemochrome non-equilibrium conformation in partially reduced human methemoglobin. A pulse-radiolysis study of aqueous-methanol solutions of methemoglobin.
The effect of external parameters on the relaxation process of the hemochrome-type non-equilibrium conformation in partially reduced methemoglobin has been investigated. The relaxation of the intermediate ferrous low-spin state to the high-spin equilibrium conformation of hemoglobin appears to be facilitated particularly by protons and phosphate ions. In addition to studying the spin-state transition in aquomethemoglobin we have also studied it in complexes of the heme group in methemoglobin with fluoride, azide and cyanide anions.
D003201:Computers; D004578:Electron Spin Resonance Spectroscopy; D006418:Heme; D006801:Humans; D007700:Kinetics; D008706:Methemoglobin; D010710:Phosphates; D011487:Protein Conformation; D011675:Pulse Radiolysis
D010710:Phosphates; D006418:Heme; D008706:Methemoglobin