BBA - Proteins and Proteomics - Carbonic Anhydrase and Superoxide Dismutase

BBA - Proteins and Proteomics  
External linkExternal link  Carbonic Anhydrase and Superoxide Dismutase
Edited by D. Silverman
Volume 1804, Issue 2, Pages 243-426 (February 2010)

This Special Edition is a collection of very interesting articles on catalysis by superoxide dismutase (SOD) and carbonic anhydrase (CA). It may seem at first that this is an arbitrary combination of two very dissimilar enzymes. However, on further consideration, there are fascinating similarities that make a valuable and informative comparison. Both SODs and CAs provide sufficient survival advantage for nature to have evolved these enzymes along several separate pathways. That is, there are classes of both SODs and CAs that are excellent examples of convergent evolution. Each member of these classes is a metalloenzyme, and of further interest is the range of metal ions that in nature are incorporated into the catalytic mechanism: Cu, Ni, Mn, and Fe for SOD and Zn, Fe, and Cd for CA.

 
David Silverman received his Ph.D. working with Ben Dailey at Columbia University on magnetic resonance spectra of molecules partially oriented in liquid crystal solvents. Postdoctoral studies followed with Harold A. Scheraga at Cornell University on protein folding and magnetic resonance of biopolymers. Silverman was recruited to the University of Florida in 1971 by Thomas H. Maren as an assistant professor and is currently a Distinguished Professor. The Silverman lab has used many approaches in the study of the mechanism of proton transfer in carbonic anhydrase and superoxide dismutase. His lab has also promoted a mass spectrometric method to measure the reactions of nitric oxide in solution.

 


  
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