Biomaterial Database

The heme environment of leghemoglobins. Absorption and circular dichroism spectra of artificial leghemoglobins and myoglobins. 1980

U Perttilä, and G Sievers

Artificial leghemoglobins were reconstituted from apoleghemoglobin and meso-, deutero- and diacetyldeuteroheme. Absorption and circular dichroism spectra of their high-spin and low-spin derivatives in the ferrous and ferric forms were recorded in the ultraviolet and visible wavelength regions. The substitution of the 2,4-side-chains of heme induced changes in the optical activity, reflecting alterations in the heme environment. The effect on the conformation of aromatic amino acid residues around heme obviously correlates with the sixth axial ligand and the spin state of iron. Absorption and CD spectra of the aquoferric derivatives of artificial myoglobins were recorded in comparison. Strongly electron-withdrawing acetyl side-chains at the 2,4-positions of diacetyldeuteroheme caused a change in the absorption spectra of aquoferric leghemoglobin and myoglobin towards low spin. On the basis of the spectra it was suggested that the displacement of the ferric iron from the pyrrole plane in leghemoglobin derivatives would be smaller than in the corresponding myoglobin derivatives.

UI	MeSH Term	Description	Entries
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
D008024	Ligands	A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)	Ligand
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.
D002942	Circular Dichroism	A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)	Circular Dichroism, Vibrational,Dichroism, Circular,Vibrational Circular Dichroism
D006418	Heme	The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.	Ferroprotoporphyrin,Protoheme,Haem,Heme b,Protoheme IX
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
D006736	Horses	Large, hoofed mammals of the family EQUIDAE. Horses are active day and night with most of the day spent seeking and consuming food. Feeding peaks occur in the early morning and late afternoon, and there are several daily periods of rest.	Equus caballus,Equus przewalskii,Horse, Domestic,Domestic Horse,Domestic Horses,Horse,Horses, Domestic
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.