Abstract
Examination of the optical and EPR properties of the ferric form of the iron containing superoxide dismutase from E.coli B, at pH values ranging from 4.5 to 10.9, has revealed two reversible structural transitions affecting the Fe/sup 3 +/ ion. The apparent pKsub(a) values of these transitions are 5.1+-0.3 and 9.O+-0.3. The binding of azide has been studied over the pH range 4.5 to 10.7; the affinity of the Fe/sup 3 +/ for N/sub 3//sup -/ is independent of pH from 4.5 to approximately 7.5, after which the dissociation constant decreased by a factor of 10 per unit increase in pH. The apparent pKsub(a) which affects N/sub 3//sup -/ binding to the iron is 8.6+-0.2. The association of N/sub 3//sup -/ with the iron has been examined using the temperature-jump method at pH 7.4 and 9.3. The kinetics of ligand association were shown to conform to the minimal mechanism: P-Fe/sup 3 +/ + N/sub 3//sup -/reversible K/sub 1/N/sub 3//sup -/ - P-Fe/sup 3 +/reversible K/sub 2/P-Fe/sup 3 +/ - N/sub 3//sup -/. K/sub 1/ was found to be essentially unaffected by pH whereas K/sub 2/ was much lower at pH 9.3 than at 7.4. The value of K/sub 1/ at
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Fee, J A;
McClune, G J;
Lees, A C;
[1]
Zidovetzki, R;
Pecht, I
[2]
- Michigan Univ., Ann Arbor (USA). Dept. of Biological Chemistry
- Weizmann Inst. of Science, Rehovoth (Israel). Dept. of Chemical Immunology
Citation Formats
Fee, J A, McClune, G J, Lees, A C, Zidovetzki, R, and Pecht, I.
PH dependence of the spectral and anion binding properties of iron containing superoxide dismutase from E. coli B. An explanation for the azide inhibition of dismutase activity.
Israel: N. p.,
1981.
Web.
Fee, J A, McClune, G J, Lees, A C, Zidovetzki, R, & Pecht, I.
PH dependence of the spectral and anion binding properties of iron containing superoxide dismutase from E. coli B. An explanation for the azide inhibition of dismutase activity.
Israel.
Fee, J A, McClune, G J, Lees, A C, Zidovetzki, R, and Pecht, I.
1981.
"PH dependence of the spectral and anion binding properties of iron containing superoxide dismutase from E. coli B. An explanation for the azide inhibition of dismutase activity."
Israel.
@misc{etde_5639782,
title = {PH dependence of the spectral and anion binding properties of iron containing superoxide dismutase from E. coli B. An explanation for the azide inhibition of dismutase activity}
author = {Fee, J A, McClune, G J, Lees, A C, Zidovetzki, R, and Pecht, I}
abstractNote = {Examination of the optical and EPR properties of the ferric form of the iron containing superoxide dismutase from E.coli B, at pH values ranging from 4.5 to 10.9, has revealed two reversible structural transitions affecting the Fe/sup 3 +/ ion. The apparent pKsub(a) values of these transitions are 5.1+-0.3 and 9.O+-0.3. The binding of azide has been studied over the pH range 4.5 to 10.7; the affinity of the Fe/sup 3 +/ for N/sub 3//sup -/ is independent of pH from 4.5 to approximately 7.5, after which the dissociation constant decreased by a factor of 10 per unit increase in pH. The apparent pKsub(a) which affects N/sub 3//sup -/ binding to the iron is 8.6+-0.2. The association of N/sub 3//sup -/ with the iron has been examined using the temperature-jump method at pH 7.4 and 9.3. The kinetics of ligand association were shown to conform to the minimal mechanism: P-Fe/sup 3 +/ + N/sub 3//sup -/reversible K/sub 1/N/sub 3//sup -/ - P-Fe/sup 3 +/reversible K/sub 2/P-Fe/sup 3 +/ - N/sub 3//sup -/. K/sub 1/ was found to be essentially unaffected by pH whereas K/sub 2/ was much lower at pH 9.3 than at 7.4. The value of K/sub 1/ at pH 7.4 (100 M/sup -1/) corresponds very closely to that obtained for the inhibition constant of azide, 10mM. A scheme is presented in which N/sub 3//sup -/ inhibits the iron containing dismutase by competing with O/sub 2//sup -/ for an anion binding site near, but not on the Fe/sup 3 +/.}
journal = []
volume = {21:1}
journal type = {AC}
place = {Israel}
year = {1981}
month = {Jan}
}
title = {PH dependence of the spectral and anion binding properties of iron containing superoxide dismutase from E. coli B. An explanation for the azide inhibition of dismutase activity}
author = {Fee, J A, McClune, G J, Lees, A C, Zidovetzki, R, and Pecht, I}
abstractNote = {Examination of the optical and EPR properties of the ferric form of the iron containing superoxide dismutase from E.coli B, at pH values ranging from 4.5 to 10.9, has revealed two reversible structural transitions affecting the Fe/sup 3 +/ ion. The apparent pKsub(a) values of these transitions are 5.1+-0.3 and 9.O+-0.3. The binding of azide has been studied over the pH range 4.5 to 10.7; the affinity of the Fe/sup 3 +/ for N/sub 3//sup -/ is independent of pH from 4.5 to approximately 7.5, after which the dissociation constant decreased by a factor of 10 per unit increase in pH. The apparent pKsub(a) which affects N/sub 3//sup -/ binding to the iron is 8.6+-0.2. The association of N/sub 3//sup -/ with the iron has been examined using the temperature-jump method at pH 7.4 and 9.3. The kinetics of ligand association were shown to conform to the minimal mechanism: P-Fe/sup 3 +/ + N/sub 3//sup -/reversible K/sub 1/N/sub 3//sup -/ - P-Fe/sup 3 +/reversible K/sub 2/P-Fe/sup 3 +/ - N/sub 3//sup -/. K/sub 1/ was found to be essentially unaffected by pH whereas K/sub 2/ was much lower at pH 9.3 than at 7.4. The value of K/sub 1/ at pH 7.4 (100 M/sup -1/) corresponds very closely to that obtained for the inhibition constant of azide, 10mM. A scheme is presented in which N/sub 3//sup -/ inhibits the iron containing dismutase by competing with O/sub 2//sup -/ for an anion binding site near, but not on the Fe/sup 3 +/.}
journal = []
volume = {21:1}
journal type = {AC}
place = {Israel}
year = {1981}
month = {Jan}
}