Biomaterial Database

Study of the pseudoperoxidatic activity of soybean leghemoglobin and sperm whale myoglobin. 1978

G Sievers, and M Rönnberg

The compound formation between soybean leghemoglobins a and c and H2O2 or ethyl hydroperoxide has been studied and compared with the hydrogen peroxide compound of sperm whale myoglobin. the titration data show that the hydrogen peroxide compounds of leghemoglobins are formed in a 1:1 molar ratio. The kinetics of the formation of the compounds follow first-order kinetics and the compounds are formed considerably faster than the myoglobin peroxide compound. The pseudoperoxidatic activity of leghemoglobins a and c and myoglobin was studied using guaiacol as electron donor. The maximal reaction velocities of leghemoglobins are greater than that of myoglobin. The results indicate that the peroxidatic activity of ferrileghemoglobin may be biologically important for instance in aging root nodules.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D007874	Leghemoglobin	A hemoglobin-like oxygen-binding hemeprotein present in the nitrogen-fixing root nodules of leguminous plants. The red pigment has a molecular weight approximately 1/4 that of hemoglobin and has been suggested to act as an oxido-reduction catalyst in symbiotic nitrogen fixation.	Leghemoglobin A
D009211	Myoglobin	A conjugated protein which is the oxygen-transporting pigment of muscle. It is made up of one globin polypeptide chain and one heme group.
D010084	Oxidation-Reduction	A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).	Redox,Oxidation Reduction
D006420	Hemeproteins	Proteins that contain an iron-porphyrin, or heme, prosthetic group resembling that of hemoglobin. (From Lehninger, Principles of Biochemistry, 1982, p480)	Hemeprotein,Heme Protein,Heme Proteins,Protein, Heme,Proteins, Heme
D006735	Horseradish Peroxidase	An enzyme isolated from horseradish which is able to act as an antigen. It is frequently used as a histochemical tracer for light and electron microscopy. Its antigenicity has permitted its use as a combined antigen and marker in experimental immunology.	Alpha-Peroxidase,Ferrihorseradish Peroxidase,Horseradish Peroxidase II,Horseradish Peroxidase III,Alpha Peroxidase,II, Horseradish Peroxidase,III, Horseradish Peroxidase,Peroxidase II, Horseradish,Peroxidase III, Horseradish,Peroxidase, Ferrihorseradish,Peroxidase, Horseradish
D006861	Hydrogen Peroxide	A strong oxidizing agent used in aqueous solution as a ripening agent, bleach, and topical anti-infective. It is relatively unstable and solutions deteriorate over time unless stabilized by the addition of acetanilide or similar organic materials.	Hydrogen Peroxide (H2O2),Hydroperoxide,Oxydol,Perhydrol,Superoxol,Peroxide, Hydrogen
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D013025	Glycine max	An annual legume. The SEEDS of this plant are edible and used to produce a variety of SOY FOODS.	Soy Beans,Soybeans,Bean, Soy,Beans, Soy,Soy Bean,Soybean
D013053	Spectrophotometry	The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.