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In plants, resins, fats, waxes, and complex organic chemicals are exuded from plants, e.g., the latex from rubber trees and milkweeds. Solid waste products may be manufactured as organic pigments derived from breakdown of pigments like hemoglobin, and inorganic salts like carbonates, bicarbonates, and phosphate, whether in ionic or in molecular ...
Leghemoglobin (also leghaemoglobin or legoglobin) is an oxygen-carrying phytoglobin found in the nitrogen-fixing root nodules of leguminous plants. It is produced by these plants in response to the roots being colonized by nitrogen-fixing bacteria, termed rhizobia, as part of the symbiotic interaction between plant and bacterium: roots not colonized by Rhizobium do not synthesise leghemoglobin.
For example, the ability of hemoglobin to effectively deliver oxygen to tissues is due to specific amino acid residues located near the heme molecule. [13] Hemoglobin reversibly binds to oxygen in the lungs when the pH is high, and the carbon dioxide concentration is low. When the situation is reversed (low pH and high carbon dioxide ...
Phytoglobins are globular plant (algae and land plant) proteins classified into the globin superfamily, which contain a heme, i.e. protoporphyrin IX-Fe, prosthetic group.The earliest known phytoglobins are leghemoglobins, discovered in 1939 by Kubo after spectroscopic and chemical analysis of the red pigment of soybean root nodules. [1]
The degradation of heme forms three distinct chromogens as seen in healing cycle of a bruise (note: the standard structure of heme is mirrored in this image, the alpha-methine bridge carbon (c5) is at the top of the structure and the beta methine-bridge carbon (c10) is counterclockwise to the left)
For example, one pathway may be responsible for the synthesis of a particular amino acid, but the breakdown of that amino acid may occur via a separate and distinct pathway. One example of an exception to this "rule" is the metabolism of glucose. Glycolysis results in the breakdown of glucose, but several reactions in the glycolysis pathway are ...
Oxidation and reduction pathways of methemoglobin and hemoglobin. Published by N. De Crem et al., 2022. In living organisms, because methemoglobin (MetHb) is unable to bind oxygen, it must be reduced to hemoglobin (Hb) through the action of the soluble isoform of cytochrome b5 reductase.
Hemoglobin in the blood carries oxygen from the respiratory organs (lungs or gills) to the other tissues of the body, where it releases the oxygen to enable aerobic respiration which powers an animal's metabolism. A healthy human has 12 to 20 grams of hemoglobin in every 100 mL of blood. Hemoglobin is a metalloprotein, a chromoprotein, and ...