-
It’s sensitive to pH, so it absorbs oxygen more readily in the lungs, and releases it slightly more near tissues that need it, as they have co2 which slightly acidifies the blood in solution (h2co3).
-
It’s effective and well tuned for our biology, it doesn’t bond strongly, and is well suited for the air-blood interface, unlike others that often favor water-blood or water-the fluid worms use instead.
Comment on Colours of Blood
lambdabeta@lemmy.ca 3 weeks ago
Whenever I see this image I always wonder 2 things:
- What makes hemoglobin more efficient?
- Why do we even need these fancy molecules to transport oxygen? Can’t we produce some kind of biological ampule that holds some pure O2 for consumption by the various processes that need it? We have dedicated organelle structures for similar tasks (i.e. mitochondria)
InverseParallax@lemmy.world 3 weeks ago
lambdabeta@lemmy.ca 3 weeks ago
Thank you. Clear, easily understood explanations of questions I always wondered. 👍🏼
BreadOven@lemmy.world 3 weeks ago
CO2 and H2CO3 (apparently I don’t know how to do subscript on here.
InverseParallax@lemmy.world 3 weeks ago
Yeah, I didn’t do the carbonic acid, then there’s the increased bicarb buffering around the pleura, couple other facts.
www.ncbi.nlm.nih.gov/books/NBK539815/
Upon entrance into red blood cells, carbon dioxide is quickly converted to carbonic acid by the enzyme carbonic anhydrase. Carbonic acid immediately dissociates into bicarbonate and hydrogen ions. As previously stated, an increase in hydrogen ions stabilize the hemoglobin in the T-state and induces oxygen unloading which leads to shifting of the dissociation curve to the right.[6]
Thus the acidity causes o2 release. Temperature (lungs tend to be very cold in the body) is important too.
Oxygen unloading is favored at higher temperatures which will cause a rightward shift. On the other hand, lower temperatures will cause a leftward shift in the dissociation curve. A notable example of this is exercise, where the temperature of muscle increases secondary to its utilization, thus shifting the curve to the right and allowing oxygen to be more easily unloaded from hemoglobin and deliver to tissues in need.
It’s amazing how subtly it works to gently increase efficiency where we need it. Otherwise it’s just a very weak oxygen bond (which is hard enough given oxygen is extremely non-polar and all you have are the valence pairs.
www.jbc.org/article/…/fulltext
Wow, I’m impressed, they’re using spin-coupling which is a pretty dicey effect.
Thus, we can conclude that the facile binding of O2 to hemo- and myoglobin arises primarily as an effect of the topology of the binding curves for the four relevant spin states. This topology, with nearly degenerat>e and parallel curves, is caused by the near degeneracy (within 10 kJ/mol) of the triplet and quintet states of deoxyheme. Therefore, the design by nature of iron porphines having close-lying spin states of a particular symmetry and energy is a means to tune binding of small ligands and overcome the activation barriers of these spin-forbidden reactions, despite the moderate SOC of first-row transition metals. The resulting barrier height makes up most of the rate enhancement due to the exponential dependence on the rate, whereas one or two orders of magnitude may come from the increase in the transmission coefficient.
That’s some fucking crazy ass engineering by nature, A weak, highly reversible bond with the molecule keyed to both pH and thermal triggers. That was a fun rabbit hole.
Macros@discuss.tchncs.de 3 weeks ago
Thanks so much for the deep dive. I love learning from such concise facts.
To add, also @Semjaza@lemmynsfw.com : There is only one known species of vertebrates without hemoglobin. The Crocodile Icefish, it once had it in its blood and lost some genes to synthesize it. The debate about why is still ongoing, with the currently favored theory that they adapted to a high oxygen and low iron environment.
TargaryenTKE@lemmy.world 3 weeks ago