to hold cargo or people. It is evident that, because of these similarities, every one of these vehicles was designed for a specific purpose and possesses common features in line with that purpose. Hemoglobin and myoglobin are molecules designed for a similar purpose, for which reason they have similar features.
A food mixer and a concrete mixer were designed for similar purposes.
• When we look at the NAS claim in a little more detail, its impossible nature can be seen more clearly. According to the claim, myoglobin gradually evolved as a result of mutations, differences formed in the amino-acid sequence, and thus the hemoglobin molecule emerged. However, we know that both myoglobin and hemoglobin possess exceedingly complex structures. If either of these molecules is subjected to random factors like mutation, the molecule's function will be corrupted, as we saw in the chapter on mutations, and it will become useless. The disease known as sickle-cell anemia is one example of this. Therefore, to expect a mutation which randomly changes a protein's amino-acid sequence to turn that protein into a more complex one with more features is to believe in the impossible. In order to prove the evolutionist claims, every transitional stage between myoglobin and hemoglobin needs to be functional (and more advantageous than the preceding stage), and that is impossible.
The American chemist Dr. Robert Kofahl, a critic of the theory of evolution, makes the following comment on the impossibility of the claim that hemoglobin evolved from myoglobin:
The structure of a hemoglobin molecule
A good example of alleged molecular homology is afforded by the a- and b- haemoglobin molecules of land vertebrates, including man. These supposedly are homologous with an ancestral myoglobin molecule similar to human myoglobin. Two a- and two b- haemoglobin associate together to form the marvelous human hemoglobin molecule that carries oxygen and carbon dioxide in our blood. But myoglobin acts as single molecules to transport oxygen in our muscles. Supposedly, the ancient original myoglobin molecules slowly evolved along two paths until the precisely designed a- and b- haemoglobin molecules resulted that function only when linked together in groups of four to work in the blood in a much different way under very different conditions from myoglobin in the muscle cells. What we have today in modern myoglobin and haemoglobin molecules are marvels of perfect designs for special, highly demanding tasks. Is there any evidence that intermediate, half-evolved molecules could have served useful functions during this imaginary evolutionary change process, or that any creature could survive with them in its blood? There is no such information. Modern vertebrates can tolerate very little variation in these molecules. Thus, the supposed evolutionary history of the allegedly homologous globin molecules is a fantasy, not science.1
As Dr. Kofahl makes clear, the NAS's claims regarding molecular homology are not science at all, but merely fantasy, like all its other claims.
Moreover, the evolutionists' accounts fail to explain the origin of the myoglobin protein. They say that hemoglobin evolved from myoglobin, but how myoglobin came into existence is still a mystery to them.
Molecular Comparisons Conflict with The So-Called Family Tree
It is suggested in Science and Creationism that an evolutionary family tree can be drawn up by comparing the proteins in living things, such as hemoglobin, myoglobin, or cytochrome c, and that this tree will agree with the paleontological and anatomical facts. This claim is set out in these terms:
The so-called family trees obtained from analyses of such molecules as hemoglobin, myoglobin, and cytochrome c conflict both with one another and with other data.
It is astonishing that the NAS should make such a claim, ignoring important research and findings in this area. In actuality, comparisons of the molecules cited by the NAS actually represent enormous difficulties for the theory of evolution and reveal its inconsistencies. Before examinin