  The evolution of terrestrial and aquatic wild type (WT) globins is dominated
by changes in two proximate - distal Histidine ligand exit channels, here
monitored quantitatively by hydropathic waves. These waves reveal allometric
functional features inaccessible to single amino acid stereochemical contact
models, and even very large all-atom Newtonian simulations. The evolutionary
differences between these features between myoglobin and neuroglobin are
related to the two oxidation channels through hydropathic wave analysis, which
identifies subtle interspecies functional differences inaccessible to
traditional size and metabolic scaling studies. Our analysis involves dynamic
synchronization of allometric interactions across entire globins.
