Studies on the Reconstitution of Bovine Erythrocyte Superoxide Dismutase

摘要: Abstract Two metal derivatives of superoxide dismutase have been prepared and partially characterized by optical, circular dichroic (CD), EPR spectroscopies. Only 2 Co(II) ions will bind to apo evidence is presented that these occupy the zinc-binding sites protein molecule. This derivative, referred as 2Co protein, has an absorption maximum at 583 nm with each ion having a molar absorbance ∼370. The CD spectrum possesses least two weak negative bands near 585 530 nm. below 100°K shows g⊥ = 4 g|| 2.16 resonances. Addition meq Cu(II) over period 1 24 hours results in formation complex which appears be bound its native position. 2Co2Cu 680 index ∼150 liters per mole cm. this derivative maxima 568 598 nm, latter 370. Evidence optical spectra are not sum appropriate proteins; thus, spectral properties depend on presence other. 20 30% can detected spectroscopy. Similarly, only portion observed helium temperatures. However, reduction signal intensity parameters similar protein. Thus, must quite close one another derivative. By analogy, supports our previous contention zinc copper copper-zinc pairs (Fee, J. A., Gaber, B. P. (1972) Biol. Chem. 247, 60).