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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.
Phytogbs0, 1, 2 and 3 are synthesized at very low concentrations in diverse (embryonic and vegetative) plant organs. [19] [20] [21] However, concentrations of Phytogbs increase in plants subjected to specific stress conditions, such as flooding [22] and light-limitation. [23] Hence, some Phytogbs have been considered as plant stress-responsive ...
Although the fold of the globin superfamily is highly evolutionarily conserved, the sequences that form the fold can have as low as 16% sequence identity. While the sequence specificity of the fold is not stringent, the hydrophobic core of the protein must be maintained and hydrophobic patches on the generally hydrophilic solvent-exposed ...
Plant nutrition is the study of the chemical elements and compounds necessary for plant growth and reproduction, plant metabolism and their external supply. In its absence the plant is unable to complete a normal life cycle, or that the element is part of some essential plant constituent or metabolite .
Selenium, which is an essential element for animals and prokaryotes and is a beneficial element for many plants, is the least-common of all the elements essential to life. [ 3 ] [ 63 ] Selenium acts as the catalytic center of several antioxidant enzymes, such as glutathione peroxidase , [ 11 ] and plays a wide variety of other biological roles .
Carbon monoxide and [[phosphorus trifluoride¿†¿ ]] are poisonous to humans because they bind to hemoglobin similarly to oxygen, but with much more strength, so that oxygen can no longer be transported throughout the body. Hemoglobin bound to carbon monoxide is known as carboxyhemoglobin.
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It is the phenomenon where an increased proton or carbon dioxide concentration (lower pH) lowers hemoglobin's affinity and carrying capacity for oxygen. [1] [2] The Root effect is to be distinguished from the Bohr effect where only the affinity to oxygen is reduced. Hemoglobins showing the Root effect show a loss of cooperativity at low pH.