The nickel(II) derivative of carbonic anhydrase and its adducts with inhii itors have been investigated through electronic and nuclear magnetic resonance (mnrj spectroscopy. The metal ion in the pure enzyme is six-coordinated, and the\* is evidence for at least one water molecule in the coordination
Characterization of cobalt(II) bovine carbonic anhydrase and of its derivatives
β Scribed by Bertini, I.; Canti, G.; Luchinat, C.; Scozzafava, A.
- Book ID
- 120485876
- Publisher
- American Chemical Society
- Year
- 1978
- Tongue
- English
- Weight
- 584 KB
- Volume
- 100
- Category
- Article
- ISSN
- 0002-7863
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The affinity of bicarboxylate ions (from oxaiate to glutarate) for cobalt(E) bovine carbonic anhydrase has been investigated and compared with that cf acetate and propionate. The oxalate ion shows a much greater affiiity for the enzyme than acetate. whereas the other bicarboxylate ions have very lit
The results of a study on the interaction between cobalt(II) bovine carbonic anhydrase and the a-amino acids L(s) and D(-Manine. glycine and betaine are reported\_ L(+)ahnine and glycine base been found to have larger aftinity for the enzyme than II(-) alanine whereas no sizable affinity is shown by
## Abstract We have attempted to elucidate the mechanism of the acquisition of activeβsite conformation in enzymes by studying the unfolding and refolding of Co(II) carbonic anhydrase. This enzyme possesses characteristic absorption and CD spectra in the visible region, which reflect primarily the