Investigation of Human Erythrocyte Superoxide Dismutase by 1H Nuclear-magnetic-resonance Spectroscopy

Overview

Journal Biochem J

Specialty Biochemistry

Date 1980 Jan 1

PMID 7378050

Authors

H A Hill

W K Lee

J V. Bannister

W H BANNISTER

Affiliations

Soon will be listed here.

Abstract

The 170MHZ 1 H n.m.r. spectra of the Cu(II)/Zn(II), Cu(I)/Zn(II) and apo- forms of human erythrocyte superoxide dismutase (EC 1.15.1.1) are reported. Resonances are assigned to the C-2 and C-4 protons of histidine residues in the active site, and it is suggested that five or six histidine residues serve as ligands to the metal ions in each subunit of the enzyme. The remaining assigned resonances are associated with histidine-41, N-terminal N-acetyl group, histidine- 108 and cysteine- 109. A comparison of the n.m.r. spectra of human and bovine superoxide dismutases suggests significant structural homology.

References

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