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The evolution of terrestrial and aquatic wild type (WT) globins is dominatedby changes in two proximate - distal Histidine ligand exit channels, heremonitored quantitatively by hydropathic waves. These waves reveal allometricfunctional features inaccessible to single amino acid stereochemical contactmodels, and even very large all-atom Newtonian simulations. The evolutionarydifferences between these features between myoglobin and neuroglobin arerelated to the two oxidation channels through hydropathic wave analysis, whichidentifies subtle interspecies functional differences inaccessible totraditional size and metabolic scaling studies. Our analysis involves dynamicsynchronization of allometric interactions across entire globins.

Oxygen Channels and Fractal Wave-Particle Duality in the Evolution of Myoglobin and Neuroglobin