F. Parak et Ve. Prusakov, RELAXATION OF NONEQUILIBRIUM STATES OF MYOGLOBIN STUDIED BY MOSSBAUER-SPECTROSCOPY, Hyperfine interactions, 91(1-4), 1994, pp. 885-890
A metastable Fe(II) low-spin myoglobin complex with H2O at the sixth c
oordination place has been produced by X-ray irradiation of metmyoglob
in at 80 K. The relaxation into the equilibrium state of deoxymyoglobi
n was investigated as a function of temperature. It starts at temperat
ures above 140 K and cannot be understood by assuming one well-defined
activation energy. The relaxation is, however, well described by assu
ming a Gaussian barrier height distribution.