Characterization of the properties of the multiple metal binding sites in alkaline phosphatase by carbon-13 nuclear magnetic resonance

Biochemistry ◽  
1980 ◽  
Vol 19 (17) ◽  
pp. 4021-4030 ◽  
Author(s):  
James D. Otvos ◽  
Ian M. Armitage
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Alkaline Phosphatase ◽  
Magnetic Resonance ◽  
Metal Binding ◽  
Binding Sites ◽  
Metal Binding Sites ◽  
Nuclear Magnetic

A Nuclear Magnetic Resonance Study of the Metal Binding Sites in Bacitracin

1975 ◽  
Vol 53 (12) ◽  
pp. 1250-1254 ◽  
Author(s):  
Roderick E. Wasylishen ◽  
Moira R. Graham
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Metal Binding ◽  
Binding Sites ◽  
Imidazole Ring ◽  
Nuclear Magnetic Resonance Study ◽  
Resonance Spectroscopy ◽  
Metal Binding Sites ◽  
Ph Values ◽  
Nuclear Magnetic

Carbon-13 nuclear magnetic resonance spectroscopy has been used to identify sites in bacitracin which bind Cu2+ and Mn2+. Results are presented which implicate the free carboxyl groups of the aspartic and glutamic acid residues and the imidazole ring of the histidine residue as metal complexation sites between pH 6 and 8. Evidence is presented which also indicates that the thiazoline ring of bacitracin binds Mn2+. Bacitracin does not bind Cu2+ or Mn2+ at pH values of 2.5 or less.

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