Metal Site Structure in a Protein Studied by Differential Perturbed Angular Correlations
- 18 February 1974
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review Letters
- Vol. 32 (7), 340-342
- https://doi.org/10.1103/PhysRevLett.32.340
Abstract
A static quadrupole interaction has been determined for the 247-keV state of bound to the active site of human carbonic anhydrase . The rotational diffusion was slowed down by dissolving the enzyme in a 46% sucrose solution at 22°C. The result yields two different frequencies and asymmetries, indicating either two forms of the enzyme or an additional site for Cd.
Keywords
This publication has 10 references indexed in Scilit:
- ??-angular correlations perturbed by stochastic fluctuating fieldsThe European Physical Journal A, 1973
- The Catalytic Mechanism of Carbonic AnhydraseProceedings of the National Academy of Sciences, 1973
- The location of tryptophanyl groups in human and bovine carbonic anhydrases: Ultraviolet difference spectra and chemical modificationBiochimica et Biophysica Acta (BBA) - Protein Structure, 1973
- Effect of Slow Rotational Diffusion on Angular CorrelationsThe Journal of Chemical Physics, 1972
- Nuclear magnetic resonance studies of bovine carbonic anhydrase. Binding of sulfonamides to the zinc enzymeBiochemistry, 1971
- Inhibition and Modification of Human Carbonic Anhydrase B with Bromoacetate and IodoacetamideEuropean Journal of Biochemistry, 1970
- STUDY OF CARBONIC ANHYDRASE USING PERTURBED ANGULAR CORRELATIONS OF GAMMA RADIATIONProceedings of the National Academy of Sciences of the United States of America, 1969
- Human Carbonic Anhydrase. Protein Conformation and Metal Ion Binding*Biochemistry, 1965
- Radiochemical Separations of CadmiumAnalytical Chemistry, 1959
- Contamination in Trace Element Analysis and its ControlMethods of biochemical analysis, 1957