113Cd NMR as a probe of the active sites of metalloenzymes

Ian M Armitage, Antonius J.M. Schoot Uiterkamp, Jan F. Chlebowski, Joseph E. Coleman

Research output: Contribution to journalArticlepeer-review

75 Scopus citations

Abstract

113Cd NMR has been used to study the active site metal ion(s) of the 113Cd(II) derivatives of four Zn(II) metalloenzymes, carboxypeptidase A, carbonic anhydrases, alkaline phosphatase, and superoxide dismutase. The resonances of the enzyme-bound 113Cd(II) ions are extremely sensitive to ligand exchange, including solvent and inhibitor, and to changes in the metal ion coordination sphere. The nature of this behavior can be shown to parallel the known structural properties and proposed roles of the metal ion in the catalytic mechanisms. Models accounting for the exchange mechanisms which may be modulating the chemical shift, linewidth, and coupling are discussed.

Original languageEnglish (US)
Pages (from-to)375-392
Number of pages18
JournalJournal of Magnetic Resonance (1969)
Volume29
Issue number2
DOIs
StatePublished - Feb 1978

Bibliographical note

Funding Information:
* Supported by Grants AM 09070-13 and AM 18778-02 from the National Institutes of Health and Grant PCM 76-8223 1 from the National Science Foundation. Acknowledgment is made to the donors of the Petroleum Research Fund, administered by the American Chemical Society, for partial support of this research and to Research Corporation.

Fingerprint Dive into the research topics of '<sup>113</sup>Cd NMR as a probe of the active sites of metalloenzymes'. Together they form a unique fingerprint.

Cite this