Superoxide dismutase activity in the giant hemoglobin of the earthworm, Lumbricus terrestris. 1996

S I Liochev, and A R Kuchumov, and S N Vinogradov, and I Fridovich
Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA.

The giant hemoglobin, which occurs in free solution in the blood of earthworms, contains copper and zinc and exhibits superoxide dismutase activity as assessed by competition assays using cytochrome c or nitroblue tetrazolium. On a molar basis, the activity of this hemoglobin was approximately 10% that of the mammalian copper, zinc superoxide dismutase. The dodecamer, which contains the globin chains but lacks the linker subunits, had very little activity when compared to the complete native molecule. This suggests that the superoxide dismutase activity resides in one of the linker subunits. This is the first report of a superoxide dismutase bound to a respiratory pigment.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
D008322 Mammals Warm-blooded vertebrate animals belonging to the class Mammalia, including all that possess hair and suckle their young. Mammalia,Mammal
D009835 Oligochaeta A class of annelid worms with few setae per segment. It includes the earthworms such as Lumbricus and Eisenia. Earthworms,Eisenia foetida,Eisenia worm,Lumbricus,Lumbricus terrestris,Eisenia fetida,Earthworm,Eisenia fetidas,Eisenia foetidas,Eisenia worms,Lumbricus terrestri,Oligochaetas,fetida, Eisenia,foetidas, Eisenia,terrestris, Lumbricus,worm, Eisenia
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D006454 Hemoglobins The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements. Eryhem,Ferrous Hemoglobin,Hemoglobin,Hemoglobin, Ferrous
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
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D013482 Superoxide Dismutase An oxidoreductase that catalyzes the reaction between SUPEROXIDES and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide. Hemocuprein,Ag-Zn Superoxide Dismutase,Cobalt Superoxide Dismutase,Cu-Superoxide Dismutase,Erythrocuprein,Fe-Superoxide Dismutase,Fe-Zn Superoxide Dismutase,Iron Superoxide Dismutase,Manganese Superoxide Dismutase,Mn-SOD,Mn-Superoxide Dismutase,Ag Zn Superoxide Dismutase,Cu Superoxide Dismutase,Dismutase, Ag-Zn Superoxide,Dismutase, Cobalt Superoxide,Dismutase, Cu-Superoxide,Dismutase, Fe-Superoxide,Dismutase, Fe-Zn Superoxide,Dismutase, Iron Superoxide,Dismutase, Manganese Superoxide,Dismutase, Mn-Superoxide,Dismutase, Superoxide,Fe Superoxide Dismutase,Fe Zn Superoxide Dismutase,Mn SOD,Mn Superoxide Dismutase,Superoxide Dismutase, Ag-Zn,Superoxide Dismutase, Cobalt,Superoxide Dismutase, Fe-Zn,Superoxide Dismutase, Iron,Superoxide Dismutase, Manganese
D015394 Molecular Structure The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds. Structure, Molecular,Molecular Structures,Structures, Molecular

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