The Amazing Design of Hemoglobin

Hemoglobin (HGB) is one of thousands of proteins designed by our Creator. We know that it carries oxygen through the bloodstream, but hemoglobin (Hgb) was designed Hgb to fulfill a number of detailed functions. Even the oxygen delivery is regulated for various needs.

Hemoglobin is an amazingly complex protein that has many functions. In the technical paper linked in this post, we can see why evolutionists cannot rationally explain it.
Credit: Pixabay / Narupon Promvichai
The intricacies of the biology of living things continue to become more amazing and complex as more research is conducted, including a surprising blood component that was recently discovered.

Believers in universal common descent evolution cannot adequately explain Hgb and its specified complexities, so they simply evosplain it away. There are also Hgb molecules produced by humans for fetal development as needed for various functions. Also, organisms that breathe air experience regulation from Hgb so that when the need for oxygen is lower (at rest), not as much is delivered. The opposite is also true. Further, the gas nitric oxide is needed and Hgb extends its extremely short half-life so it can fulfill its function. There is a great deal to learn, but this article is quite technical and people with advanced medical and biological knowledge are the ones who would receive the most benefit from it.
In this article we first examine the structure of Hgb and how this makes Hgb ideally suited as an O2 transporter. We’ll very briefly look at the genes that code for the various subunits of Hgb and how they are arranged on the chromosomes, and how their expression changes through development from embryo to adult, and how this is regulated. We will examine how hemoglobin structure enhances the binding and release of O2, making hemoglobin an exquisitely designed sensor of the metabolic demands for oxygen. We will make some comparisons between Hgb and myoglobin, another O2 binding protein found in muscle, and see how its structure suits it to be an excellent O2 storage protein in cells. We examine some associated enzymatic activities of Hgb and Mb that protect us from nitric oxide (NO), but at the same time provide a way to preserve and deliver NO to where it’s needed. We briefly look at Hgbs from other mammals and see that their Hgbs are matched to their metabolic demands. Lastly, we mention some research advances and shortcomings in attempts to make artificial Hgb to meet many medical needs.
To learn more, you can read the entire article by clicking on "Hemoglobin: An Exquisitely Designed, Multifunctional Protein".