The active site structure of Thalassiosira weissflogii carbonic anhydrase 1 |
| |
Authors: | Cox E H McLendon G L Morel F M Lane T W Prince R C Pickering I J George G N |
| |
Affiliation: | Center for Environmental Bioinorganic Chemistry, Departments of Chemistry and Geosciences, Princeton University, Princeton, New Jersey 08544, USA. |
| |
Abstract: | X-ray absorption spectroscopy at the Zn K-edge indicates that the active site of the marine diatom Thalassiosira weissflogii carbonic anhydrase is strikingly similar to that of mammalian alpha-carbonic anhydrase enzymes. The zinc has three histidine ligands and a single water at 1.98 A. This is quite different from the beta-carbonic anhydrases of higher plants in which zinc is coordinated by two cysteine thiolates, one histidine, and a water molecule. The diatom carbonic anhydrase shows no significant sequence similarity with other carbonic anhydrases and may represent an example of convergent evolution at the molecular level. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|