What color does deoxyhemoglobin appear in and how does oxygen bind to hemoglobin?

Deoxyhemoglobin mature red blood cells not only have no nucleus, but also have no organelles such as microchondria and nucleoproteosomes, and cannot carry out nucleic acid and protein biosynthesis, nor can they carry out aerobic oxidation, and cannot use fatty acids. Blood sugar is its only source of energy. Glucose uptake by red blood cells is facilitated by diffusion and is not dependent on insulin.

The metabolic pathways retained by mature erythrocytes are mainly glucose digestion and pentose phosphate pathway, as well as monodiphosphoglycerate (2,3-biphosphoglycerate, bilberry pg). These metabolisms provide energy and reducing power (NADH, NADPH) as well as some important metabolites (2,3 pyrocytes, PG), which play an important role in maintaining the vital processes and normal physiological functions of mature red blood cells in the circulation of about 120.

a) Glycolysis.

The red blood cells circulating in the blood consume about 30 g of glucose per day, of which 90-95% are utilized by glycolysis. One molecule of glucose is digested to produce two molecules of ATP. The ATP produced in red blood cells is mainly used to maintain ion pumps (sodium pumps, calcium pumps) on red blood cell membranes to maintain the ion balance of red blood cells; Maintain cell membrane plasticity; Glutathione synthesis and nucleotide salvage synthesis, etc.

In the absence of ATP, the balance of ions inside and outside the red blood cell membrane is imbalanced, and the RNA entry in the red blood cell is more than K and the excretion of CA increases, and the red blood cells swell into a spherical shape or even rupture due to excessive water inhalation. At the same time, due to ATP deficiency, the plasticity of the red blood cell membrane can be reduced, the hardness of the red blood cell can be increased, and it is easy to be destroyed by the spleen, resulting in hemolysis.

NADH H, produced in the anaerobic digestion of red blood cells, is a cofactor for methemoglobin reductase, which catalyzes the reduction of methemoglobin to oxygen-carrying hemoglobin.

b) 2,3-bisphosphoglyceric acid (2,3-bpg) branch.

In the glycanaerobic digestion pathway, 15 50% of 1,3-bisphosphoglycerate (1,3-bpg) is catalyzed by bisphoglycerate mutase to produce 2,3-bpg, which is then catalyzed by 2,3-bpg phosphatase to produce 3-phosphoglyceric acid. The collateral circulation through this 2,3-bpg is called the 2,3-bpg branch.

It's still red, and it doesn't matter if you melt oxygen or not, it's just that the oxidation ability has become weaker.

It enters the trachea from the nasal cavity or oral cavity, from the trachea to the bronchi, the bronchial segments to the alveoli, enters the capillaries through the alveolar membrane and binds to hemoglobin, and reaches the left ventricle through the pulmonary circulation called arterial blood, which enters the systemic circulation to various aerobic organs and tissues in the body.

The process by which hemoglobin combines with oxygen is a very magical process. First, an oxygen molecule binds to one of the four subunits of hemoglobin, and the globin structure changes after binding to oxygen, resulting in a change in the structure of the entire hemoglobin, which makes it easier for the second oxygen molecule to find another subunit of hemoglobin than the first oxygen molecule to bind, and its binding will further promote the binding of the third oxygen molecule, and so on until the four subunits that make up hemoglobin bind to the four oxygen molecules.

Heme molecular structure due to the synergistic effect, the binding curve of hemoglobin and oxygen is S-shaped, in a specific range with the change of oxygen content in the environment, the binding rate of hemoglobin and oxygen molecules has a drastic change process, the oxygen concentration in the tissues of the organism and the oxygen concentration in the lung tissue are just on both sides of this mutation, so in the lung tissue, hemoglobin can be fully combined with oxygen, and the oxygen molecules carried in other parts of the body can be fully released. However, when the oxygen content in the environment is very high or very low, the oxygen binding curve of hemoglobin is very flat, and the huge fluctuation of oxygen concentration is difficult to make the binding rate of hemoglobin and oxygen change significantly, so even if a healthy person breathes pure oxygen, the ability of blood to carry oxygen will not be significantly improved.

In addition to carrying oxygen, hemoglobin can also be combined with carbon dioxide, carbon monoxide, cyanide ions, and the way of binding is exactly the same as oxygen, the difference is only the firmness of the combination, carbon monoxide, cyanide ions are difficult to leave once combined with hemoglobin, this is the principle of gas poisoning and cyanide poisoning, in this case, other substances with stronger binding ability can be used to detoxify, such as carbon monoxide poisoning can be treated by intravenous injection of methylene blue.

Oxyhemoglobin is red, and deoxyhemoglobin is purplish-red.

The toxicological effect of carbon monoxide on humans is mainly the combination of hemoglobin in red blood cells Under normal circumstances, when oxygen enters the blood, it combines with hemoglobin in red blood cells to form oxyhemoglobin, which circulates with the blood

Oxyhemoglobin flows to all parts of the body, releases oxygen, and tissue cells get sufficient oxygen, however, when carbon monoxide is inhaled, it takes the lead, before oxygen and hemoglobin combine, forming carboxyhemoglobin (also known as carbon monoxide hemoglobin) At this time, although the blood circulation is in progress, the blood is full of carboxyhemoglobin, which cannot carry oxygen, and after a long time, the symptoms of tissue cell hypoxia are very obvious, and finally the human body dies due to severe hypoxic asphyxiation.

It should be mentioned that the **mucous membrane of carbon monoxide poisoning patients is cherry red, which is different from the bruising of general hypoxia, which is due to the fact that the color of carboxyhemoglobin is cherry red, so it is also reflected in the **mucosa

In the case of carbon monoxide poisoning, carboxyhemoglobin is present in the blood, so the corpse spots are cherry red;

Oxyhemoglobin (oxyhemoglobin

It is a substance produced by the reversible combination of hemoglobin and oxygen molecules. Oxyhemoglobin plays a great role in transporting oxygen to tissues.

The heme iron atom is divalent with O2, 4 N of porphyrin, and binds to the histidine residue of globin (imidazole) to form an octahedral complex structure. Unlike free hemoglobin, it is a low-spin substance, and its absorption spectrum is similar to cytochrome reduction. The plot of the partial pressure of oxygen and the percentage (%) of oxyhemoglobin formation, i.e., the binding curve (dissociation curve), is S-shaped due to the allosteric effect of the heme interaction.

Oxyhemoglobin is more acidic than hemoglobin and emits H+ when it is produced, which is called the library effect. It can be thought that it binds to oxygen in the lungs and releases carbon dioxide; In tissues, the correlation between the production of lactate and the free of oxygen is significant.

Oxyhemoglobin is a chemical synthesis of bright red hemoglobin and oxygen, which transports oxygen to tissues.

The different absorption spectra of hemoglobin to near-infrared light in different oxygenation states can be used to quantitatively detect the changes in the concentrations of oxyhemoglobin, reduced hemoglobin and cytochrome oxidase in human tissues.

It is hemoglobin that binds to oxygen.

Oxyhemoglobin is a chemical synthesis of bright red hemoglobin and oxygen, which transports oxygen to tissues.

Applied Disciplines: Biochemistry and Molecular Biology (first-level disciplines); Amino acids, peptides and protein nucleoenvy (secondary discipline).

Hemoglobin is used in different oxygenation states.

You know that hemoglobin both binds and loses oxygen easily. Oxidized hemoglobin is hemoglobin that binds to oxygen.

There is a red iron-containing protein in red blood cells, called hemoglobin The reason why red blood cells are red is because they contain hemoglobin Hemoglobin characteristics: in places with high oxygen content, it is easy to combine with oxygen; In places with low oxygen content, it is easy to separate from oxygen This virtual property of hemoglobin makes red blood cells have the function of transporting oxygen, in addition, red blood cells also transport a part of carbon dioxide

So the answer is: iron; Red talks about this; High; Low.