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

doi:10.1016/0022-2364(78)90160-9

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

Chemical and Structural Biology (TMED)

Research output: Contribution to journal › Article › peer-review

14 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 language	English (US)
Pages (from-to)	375-392
Number of pages	18
Journal	Journal of Magnetic Resonance (1969)
Volume	29
Issue number	2
DOIs	https://doi.org/10.1016/0022-2364(78)90160-9
State	Published - 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.

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10.1016/0022-2364(78)90160-9

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title = "113Cd NMR as a probe of the active sites of metalloenzymes",

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.",

author = "Armitage, {Ian M} and {Schoot Uiterkamp}, {Antonius J.M.} and Chlebowski, {Jan F.} and Coleman, {Joseph E.}",

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.",

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AU - Armitage, Ian M

AU - Schoot Uiterkamp, Antonius J.M.

AU - Chlebowski, Jan F.

AU - Coleman, Joseph E.

N1 - 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.

PY - 1978/2

Y1 - 1978/2

N2 - 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.

AB - 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.

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