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.
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