Study of dynamic characteristics of conformation non-equilibrium states of hemoglobin and its complexes by the radiolysis method

By the pulse radiolysis method dynamic characteristics of conformational non-equilibrium states of hemoglobin have been investigated, which originate in the reduction of methemoglobin and its complexes with CN- and N3- by hydrated electrons. Energy of the electrons is 4.5 MeV, duration of the electron pulse does not exceed 2 μs. Conformational nonequilibrium states of protein have been found to relax to the corresponding equilibrium states in several kinetic stages with constants of 104-101 s-1. The relaxation mechanism depends on the nature of the ligands of iron and pH of the medium. Analysis of the absorption spectra of the conformational non-eqilibrium states of hemoglobin and its complexes shows that part of the protein molecules is in low-spin state