The recent availability of X-ray structures and new biophysical measurements have shed further light on the detailed mechanism of carbonic anhydrase and its inhibition. It is noted that in some instances the structural information obtained through X-ray analysis of single crystals and NMR measurements in solution disagree. We take these conflicting results as possible conformations close in energies, both of which can be used to design the enzymatic pathway.
Bertini, I., Luchinat, C., Pierattelli, R., Mangani, S. (1995). Carbonic-anhydrase - An Example of How the Cavity Governs the Reactivity At the Zinc Ion. COMMENTS ON INORGANIC CHEMISTRY, 17(1), 1-15 [10.1080/02603599508035779].
Carbonic-anhydrase - An Example of How the Cavity Governs the Reactivity At the Zinc Ion
Mangani, Stefano
1995-01-01
Abstract
The recent availability of X-ray structures and new biophysical measurements have shed further light on the detailed mechanism of carbonic anhydrase and its inhibition. It is noted that in some instances the structural information obtained through X-ray analysis of single crystals and NMR measurements in solution disagree. We take these conflicting results as possible conformations close in energies, both of which can be used to design the enzymatic pathway.
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https://hdl.handle.net/11365/35183
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