Short answer: Cyclone technology in vacuums run on a motorized propeller. Proteins don’t.
See, the “cyclone” is produced by an electric motorized propeller with tilted wings. As it spins, it brings the air in one direction. It’s how a normal stand fan would work to bring the air towards the recipient. But this may be wrong if you are implying that hemoglobin spins around in the red blood cell. That is a very interesting possibility, but I will not delve into that yet.
Hemoglobin is a protein that has been evolving for over 3-4 billion years. And from what I’ve seen, such as the human immune system, nature has developed efficient ways to develop proteins to conduct their function efficiently.
According to the images shown in your post, hemoglobin does show some similarity to the cyclone technology used in vacuums. Most likely, this property is conducted by an electric attraction, as other proteins use this electromagnetic force to bring things together.
However, even though cyclone technology is used for degassing, 1 Hemoglobin protein can only carry very small amounts of oxygen, by the 4 iron atoms, and thos uron atoms are suspected to attract the dioxygen from the water and bond with it. One hemoglobin protein doesn’t have much capacity, so I don’t think it would need much power to gain 4 oxygen molecules.
Also, this protein must be able to repel water. Water is both negatively and positively charged, as it is a polar molecule. This can be done via hydrophobics, but consider that heme molecules haven’t been shown to react with water.
Even though hemoglobin does look fairly similar to cyclone technology, then there has to be a way to channel dissolved oxygen into hemoglobin. My theory is via diffusion.
When the oxygen gets absorbed into the capillaries by the alveoli, the blood is mostly likely going to be supersaturated with the oxygen, because in an inhalation, many, many of the oxygen atoms are absorbed from the air into the lungs. The lungs divide the oxygen into smaller doses via the bronchioles, but just enough oxygen sent into the blood stream so that the deoxygenated hemoglobin can react with the oxygen to oxygenate the hemoglobin in the red blood cells.
Also, consider that red blood cells don’t move by themselves, and flow with the blood. This dissolved oxygen has to make the journey through the water into the numerous red cells. In this case, the capillaries are very small, so the red blood cells are pretty huge relative to the width of the blood cells by then, so it is fairly easy for the oxygen to get into the red blood cells first.
If you take these reasons into consideration, proteins are not likely to have the same mechanics as cyclone technology.
One possible alternate idea for how oxygen molecules are attracted to hemoglobin is in the image below.
| [img_assist |
nid=2009625 |
title=How oxygen binds to heme molecules |
desc=This is a picture illustrating how oxygen binds to heme molecules. |
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align=center |
width=200 |
height=200] |
According to the image from biology.kenyon.edu , it appears as if the hemoglobin protein itself does not play a major role in attracting the oxygen molecules, but the heme molecule itself.
Even though the helixes are mostly polar and make up most of the protein, there is no clear diagram of amino acids that illustrate that the globin attracts the oxygen molecules in the first place.
In the heme molecule depicted in the image, it also appears as if the nitrogen donor atoms attract the oxygen molecule as well, and that the domed shape of the nitrogen-iron complex greatly focuses the oxygen molecule to be attracted, like a satellite antenna.
So, it appears as if the heme molecule is what makes the hemoglobin absorb oxygen. There is a possibility that the polar isosurface of the globin channels the oxygen molecules into the heme molecules, but there is no visible and clear evidence about that in my opinion. I think the globin is just to prevent the heme molecules from reacting abnormally.
Thank you for reading through this!