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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 R-carbonic anhydrase enzymes. The zinc has three histidine ligands and a single water at 1.98 Å. This is quite different from the -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 significantdoi:10.1021/bi001416s pmid:11015190 fatcat:ifeif6adlzbwrj4rrnmxx2stcq