Why is oxygenated hemoglobin red

Blood vessels line the perimeter of each air sack where hemoglobin inside of red blood cells rushing through the capillaries pick up their molecular cargo.

Within moments, those red blood cells have carried oxygen all the way to the tips of your fingers and toes. Hemoglobin is such an effective transporter of small molecules, it even picks up Carbon Dioxide for its return trip to the lungs.

Hemoglobin is found in more places in the body than just red blood cells. The brain requires a sensitive balance of Oxygen at all times. Since hemoglobin deftly manipulates Oxygen, certain types of neurons will access the Hemoglobin gene in its DNA and synthesize a storage device. For this reason, they have a higher demand for Oxygen.

Would you believe hemoglobin is also a protector of cells? Not in humans, or vertebrae though. In , Kjeld Marcher and Desh Pal Verma first isolated the genes that encoded for this out of place hemoglobin protein, calling it Leghemoglobins due to the remarkable similarity to mammalian hemoglobin. IMAGE It was difficult at first to conceive why a plant would make its own Oxygen transporting protein, since a legume can make its own oxygen using chlorophyll.

They speculated that these nodules contained specialized bacteria that convert nitrogen from the environment into a form the plant can use.

This sensitive cellular machinery is susceptible to damage from rampant oxygen migrating throughout the cells. Since Leghemoglobin would have a strong Oxygen affinity, Marcher and Verma speculated that the protein scavenged cells for oxygen protecting cellular machinery.

After that time, scientists have found hemoglobin proteins in every form of plant studied, even those that form no symbiotic relationship with bacteria. As far as we can tell, nearly all forms of life on the planet currently use HEME-globulin proteins to manage Oxygen molecules inside cells, either for transportation, management or protection.

Only something truly ancient could be found in life forms as diverse as bacteria, plants and animals. The 3-dimensional shape of Hemoglobin is characterized by two specific stable positions referred to as the R and T States Relaxed and Tense. Oxygenated Hemoglobin is Relaxed and flexible with a high affinity for oxygen.

De-oxygenated Hemoglobin is tense, rigid and inflexible with a low affinity for oxygen. Cooperative BindingHemoglobin is a wonderfully complex protein. This interesting adaption is all thanks to the tiny changes in the position of Iron atoms bound to the center of each HEME group. Hemoglobin is unique protein. Every single breath, we directly experience with something millions of times smaller than something we can see with our eyes; amazing to think something so small can actually cause us pain.

Its role in our body is critical to maintaining our health. A number of physiological systems impact the creation and function of Hemoglobin. It is a target for diagnostic measurement and directly connected to a number of different physiological conditions. Swapping just one amino acid for another, the mutation causes life-threatening consequences for people suffering from this condition. In its Deoxygenated form T State , these mutated Beta chains attaches to an adjacent Alpha chain of a neighboring Hemoglobin.

One after another, Hemoglobin links to creating a rigid, protein fiber. In this state, the sickled red blood cell clogs tiny capillaries, digging into and damaging tissue causing cardiovascular problems including pain!

There are many variations of hemoglobin present in different species, which allows scientists to distinguish blood samples from various animals. Over time, spilled blood that starts out red turns darker and darker as it dries and its hemoglobin breaks down into a compound called methemoglobin. As time passes, dried blood continues to change, growing even darker thanks to another compound called hemichrome.

This continual chemical and color change allows forensic scientists to determine the time a blood drop was left at a crime scene. Then using computer modeling we can estimate the time since the blood was deposited to help investigators determine if a blood stain is relevant to a crime.

If the blood is a year old, it might not be important to a crime committed yesterday. Portsmouth Climate Festival — Portsmouth, Portsmouth. Edition: Available editions United Kingdom. Blood is red because of the hemoglobin inside our red blood cells.

Hemoglobin is a protein that forms a complex with iron molecules and together they transport oxygen molecules throughout the body. Iron has the property of reflecting red light and because there is so much iron in our blood, blood looks red.

When hemoglobin is carrying a lot of oxygen like when just leaving the lungs , blood is bright red. When most of the oxygen has been released to the body, blood is dark red. Therefore, contrary to popular belief, blood is never blue. Veins under light colored skin only look blue because the skin changes the optical properties of the light that passes through the skin.

In other words, skin changes the way light is reflected from the blood and we perceive that as being a different color.