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Fluorescence and 19F NMR evidence that phenylalanine, 3-L-fluorophenylalanine and 4-L-fluorophenylalanine bind to the L-leucine specific receptor of Escherichia coli

Published online by Cambridge University Press:  10 February 2001

LINDA A. LUCK  and
COLIN JOHNSON
LINDA A. LUCK
Affiliation:
Department of Chemistry, Clarkson University, Potsdam, New York 13699
COLIN JOHNSON
Affiliation:
Department of Chemistry, Clarkson University, Potsdam, New York 13699
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Abstract

The binding capacity of the L-leucine receptor from Escherichia coli was measured with L-phenylalanine and 4-fluoro-L-phenylalanine as substrates by fluorescence. The apparent dissociation constants (KD) for L-leucine, L-phenylalanine, and 4-fluoro-L-phenylalanine are 0.40, 0.18, and 0.26 respectively. 19F NMR data show protein-induced shifts for the 4-fluoro-L-phenylalanine peak and 3-fluoro-L-phenylalanine when receptor is present. Evidence points to the binding of only the L-isomers of these fluorine analogs.

Keywords

19F NMRfluorescence3-fluoro-phenylalanine4-fluoro-phenylalanineleucineperiplasmic proteinsreceptor

Information

Type
FOR THE RECORD
Information
Protein Science , Volume 9 , Issue 12 , December 2000 , pp. 2573 - 2576
Copyright
© 2000 The Protein Society

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