Histidine → Carboxamide Ligand Substitutions in the Zinc Binding Site of Carbonic Anhydrase II Alter Metal Coordination Geometry but Retain Catalytic Activity†

Biochemistry ◽  
1997 ◽  
Vol 36 (50) ◽  
pp. 15780-15791 ◽  
Author(s):  
Charles A. Lesburg ◽  
Chih-chin Huang ◽  
David W. Christianson ◽  
Carol A. Fierke
1998 ◽  
Vol 76 (7) ◽  
pp. 1027-1032 ◽  
Author(s):  
Silvia Álvarez-Santos ◽  
Àngels González-Lafont ◽  
José M Lluch

The hydrogen bond network influence on the carbonic anhydrase II (CAII) zinc binding site has been studied theoretically by using the semiempirical AM1 method. To this aim, quantum mechanical reduced models of wild-type CAII and several CAII variants have been constructed. We have shown that, when a direct metal ligand donates a hydrogen bond to an indirect metal ligand, the first-shell residues enhance their electrostatic interaction with the zinc cation. Thus, the hydrogen-bond network is able to modulate the zinc binding affinity and the zinc-water pKa.Key words: hydrogen bond network, carbonic anhydrase II, Zn2+ metalloenzyme ligands.


Biochemistry ◽  
1993 ◽  
Vol 32 (38) ◽  
pp. 9896-9900 ◽  
Author(s):  
Laura L. Kiefer ◽  
Joseph F. Krebs ◽  
Steven A. Paterno ◽  
Carol A. Fierke

1995 ◽  
Vol 8 (10) ◽  
pp. 975-980 ◽  
Author(s):  
Joseph A. Ippolito ◽  
Satish K. Nair ◽  
Richard S. Alexander ◽  
Laura L. Kiefer ◽  
Carol A. Fierke ◽  
...  

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Na Jin Kim ◽  
Subin Kim ◽  
Semi Hong ◽  
Jongmin Sung ◽  
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Biochemistry ◽  
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pp. 6237-6244 ◽  
Author(s):  
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Silvia Tilli ◽  
Fabrizio Briganti ◽  
W. Richard Chegwidden ◽  
Claudiu T. Supuran ◽  
...  

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