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Time-resolved fluorescence studies of tryptophan mutants of Escherichia coli glutamine synthetase: conformational analysis of intermediates and transition-state complexes.

Single tryptophan-containing mutants of low adenylylation state Escherichia coli glutamine synthetase have been studied by frequency-domain fluorescence spectroscopy in the presence of various substrates and inhibitors. At pH 6.5, the Mn-bound wild-type enzyme (wild type has two tryptophans/subunit)...

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Detalhes bibliográficos
Main Authors: Atkins, W. M., Villafranca, J. J.
Formato: Artigo
Idioma:Inglês
Publicado em: Cold Spring Harbor Laboratory Press 1992
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2142202/
https://ncbi.nlm.nih.gov/pubmed/1363912
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