PMID: 41239Sep 1, 1979

pH-dependent migration of copper(II) to the vacant zinc-binding site of zinc-free bovine erythrocyte superoxide dismutase

Proceedings of the National Academy of Sciences of the United States of America
Joan Selverstone ValentineS J Lippard


Bovine erythrocyte superoxide dismutase (Cu(2)Zn(2)SODase; superoxide:superoxide oxidoreductase, EC consists of two identical subunits each containing Cu(2+) and Zn(2+) in close proximity. We describe here electron spin resonance (ESR) and visible absorption spectroscopic studies of the zinc-free derivative of this protein, Cu(2)E(2)SODase (E = empty) over the pH range 6-10. The ESR spectrum of the zinc-free protein at 77 K is markedly pH dependent. At pH < 8.0 the ESR spectrum is axial in appearance. At pH > 8.0, the lineshape becomes increasingly distorted with increasing pH until, at pH = 9.5, the spectrum is very broad and resembles that of the four-copper derivative Cu(2)Cu(2)SODase and of model imidazolate-bridged binuclear Cu(II) complexes. ESR spectra at 30 degrees C are also consistent with formation of Cu(II)-Im-Cu(II). A plot of changes in the signal amplitude of g perpendicular for Cu(2)E(2)SODase as a function of pH gives an apparent pK(a) of 8.2 for the transition. The long-wavelength absorption with lambda(max) = 700 nm characteristic of Cu(2)E(2)SODase shifts with increasing pH to 800 nm and the resulting visible spectrum is identical to that of Cu(2)Cu(2)SODase. All of the above-mentioned spectroscopi...Continue Reading


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