Leghemoglobin


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Leghemoglobin

 

a red iron-containing protein, similar in a number of properties to the hemoglobin of blood, that forms in the root nodules of actively nitrogen-fixing leguminous plants of the genus Leguminosae.

Leghemoglobin is a product of the symbiosis of two organisms: it consists of a heme synthesized by nodule bacteria and a globin formed by the cells of a higher plant. Leghemoglobin is destroyed when the nodules lose their capacity for symbiotic nitrogen fixation. Leghemoglobin was isolated in 1939 from the nodules of horse beans. It was obtained in crystalline form in 1959 from soy nodules. Like other hemoproteins, leghemoglobin regulates the oxygen regime in the nodule.

REFERENCES

Zhiznevskaia, G. Ia. Med’, molibden i zhelezo v azotnom obmene bobovykh rastenii Moscow, 1972.
Kretovich, V. L. Obmen azota v rasteniiakh. Moscow, 1972. [14–7264]
References in periodicals archive ?
Targeting of the soybean leghemoglobin to tobacco chloroplasts: Effects on aerobic metabolism in transgenic plants.
US Patent # 8,021,695 B2: Personal Care Composition Containing Leghemoglobin
Another cluster of strains were ranked as partially-effective (PE), and those producing lower nodule tissue with no visible traces of leghemoglobin were classified as ineffective (I) in fixing nitrogen.
The ability of these indigenous rhizobia to produce nodules with visible interior red pigmentation due to leghemoglobin, indicated that they were effective with a potential to establish successful symbiotic associations.
The hemoglobin found in root nodules of legumes is called leghemoglobin (leg for legume); it is now believed that this protein supplies oxygen to the bacteria while keeping it away from the nitrogen-fixing machinery to which it is toxic (9).
Leghemoglobin genes (lb) in legumes and their cDNAs have been the best-studied plant genes (Stroczycki & Logocki, 1995).
Leghemoglobins from an evolutionarily old legume, Lupinus luteus.
Leghemoglobin has mystified researchers for years because the sites where oxygen or carbon monoxide bind to heme proteins lie deeply buried and seem inaccessible.
Gruber, tyrosinase production is slowed by competitive binding of nitric oxide with the leghemoglobin present in the Lotus symbiosome lysate which removes this signaling molecule from its typical binding with guanylyl cyclase.