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Heme oxygenase, or haem oxygenase, (HMOX, commonly abbreviated as HO) is an enzyme that catalyzes the degradation of heme to produce biliverdin, ferrous iron, and carbon monoxide. [ 1 ] There are many heme degrading enzymes in nature.
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.
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 ...
RpiA plays an essential role in the metabolism of plants and animals, as it is involved in the Calvin cycle which takes place in plants, and the pentose phosphate pathway which takes place in plants as well as animals. All orthologs of the enzyme maintain an asymmetric tetramer quaternary structure with a cleft containing the active site. Each ...
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 ...
The pentose phosphate pathway. The pentose phosphate pathway (also called the phosphogluconate pathway and the hexose monophosphate shunt or HMP shunt) is a metabolic pathway parallel to glycolysis. [1] It generates NADPH and pentoses (five-carbon sugars) as well as ribose 5-phosphate, a precursor for the synthesis of nucleotides. [1]
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]
Since it was shown that VHb stimulated the growth of E. coli under hypoxic conditions, vgb was cloned into a variety of organisms, including various bacteria, yeast, fungi, and even higher plants and animals to test its effects on growth and production of products of potential commercial importance, the degradation of toxic compounds, the ...