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The 270-MHz 1H nuclear magnetic resonance spectra of the apo, copper(I)-zinc(II), and copper(II)-zinc(II) forms of bovine erythrocyte superoxide dismutase (EC 1.15.1.1) are reported, and assignments of resonances to ten amino acid residues are proposed. The data require that at least four and probably six histidine residues serve as ligands to the metals in each subunit of the enzyme, consistent with x-ray diffraction results. The remaining assigned resonances are associated with His-19, His-41, Tyr-108, and the N-terminal N-acetyl group. The imidazole C(2)H of His-41 exchanges readily at pH greater than 8. The structural implications of the effect of the paramagnetic Cu(II) in the holoenzyme on the proton relaxation times are in reasonable accord with the data from x-ray diffraction studies.
A E Cass, and
A O Hill, and
B E Smith, and
J V Bannister, and
W H Bannister
January 1980,
The Biochemical journal,
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July 1996,
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J V Bannister, and
W H Bannister
August 1979,
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A E Cass, and
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W H Bannister
June 1972,
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A E Cass, and
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March 1977,
Biochemistry,
A E Cass, and
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J V Bannister, and
W H Bannister
January 1992,
Neuroradiology,
A E Cass, and
A O Hill, and
B E Smith, and
J V Bannister, and
W H Bannister
February 1980,
Biochemistry,
A E Cass, and
A O Hill, and
B E Smith, and
J V Bannister, and
W H Bannister
October 1979,
Journal of inorganic biochemistry,
A E Cass, and
A O Hill, and
B E Smith, and
J V Bannister, and
W H Bannister
February 2002,
The Journal of dairy research,
A E Cass, and
A O Hill, and
B E Smith, and
J V Bannister, and
W H Bannister
February 1980,
Biochemistry,
