Determination of metal-metal distances in E. coli glutamine synthetase by EPR
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference17 articles.
1. Conformational changes in glutamine synthetase from Escherichia coli. I. Binding of manganese ion in relation to some aspects of the enzyme structure and activity
2. Glutamine Synthetase of Escherichia Coli: Some Physical and Chemical Properties
3. Manganese(II) and substrate interaction with unadenylylated glutamine synthetase (Escherichia coli W). I. Temperature and frequency dependent nuclear magnetic resonance studies
4. Metal ion requirement by glutamine synthetase of Escherichia coli in catalysis of γ-glutamyl transfer
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1. The Role of Metals in Enzyme-Catalyzed Substitutions at each of the Phosphorus Atoms of ATP;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
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3. Two-Metal Ion Catalysis in Enzymatic Acyl- and Phosphoryl-Transfer Reactions;Angewandte Chemie International Edition in English;1996-10-01
4. Enzymatische Acyl- und Phosphoryltransferreaktionen unter Beteiligung von zwei Metallionen;Angewandte Chemie;1996-09-20
5. A structural model for fidelity in transcription.;Proceedings of the National Academy of Sciences;1994-08-02
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