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

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. Introduction Here we discuss the evolution of myoglobin (Mb) and neuroglobin (Nb) in functional terms, connecting hydropathic allometric globular properties and oxidation kinetics. Our analysis assumes that globins have evolved from aquatic predecessors to take nearly optimal advantage of the 28 times larger oxygen concentration available terrestrially. Mb stores O2 in tissues, was the first protein whose structure was determined [1], and is the best understood globin. Nb is concentrated in the neural network and the retina, and it exhibits instructive differences from Mb, and substantial sequence differences (24% identity, 39% similarity). Features of Mb and Nb evolution are largely hidden from structural studies, which generally show little difference between human and chicken protein backbones. Phylogenetic trees explore evolution in terms of