Comparison of the behavior of sea hare myoglobin when it forms two different complexes

Sea hare myoglobin presents a chaotic behavior when it reacts with imidazole but such a behavior does not appear when it reacts with cyanide. The binding of imidazole to the sea hare myoglobin could be seen as the result of a special vibrational coupling under the control of an attractor with the correlation dimension 4.2±0.17. The Poincaré plot for the changes in the temperature factors presents a region preferentially occupied, the autocorrelation function presents the damping expected from the control of the attractor, the power spectrum is broad and the first Lyapunov coefficient is positive, L=0.045±0.003. When the myoglobin forms the complex with cyanide, the situation is a little different. Although the Poincaré plot represents the region preferentially occupied and the power spectrum is broad, in this case we can not obtain the saturation of the integral correlation coefficient with increasing number of coordinates in the phase space. The damping of the autocorrelation function is not so strong as that for the complex of myoglobin with imidazole and we can not be sure that the first Lyapunov coefficient remains positive after the progression of step number.