A Fluorescence Study of Single Tryptophan-Containing Mutants of Enzyme IImtl of the Escherichia coli Phosphoenolpyruvate-Dependent Mannitol Transport System-Reference-Cited by-同舟云学术

A Fluorescence Study of Single Tryptophan-Containing Mutants of Enzyme IImtl of the Escherichia coli Phosphoenolpyruvate-Dependent Mannitol Transport System

Published:1996-01-01 Issue:21 Volume:35 Page:6628-6634
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Swaving Dijkstra Dolf¹,Broos Jaap¹,Lolkema Juke S.¹,Enequist Hans¹,Minke Wendy¹,Robillard George T.¹

Affiliation:

1. Department of Biochemistry and Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi952222t

Reference46 articles.

1. Expression, purification, and kinetic characterization of the mannitol transport domain of the phosphoenolpyruvate-dependent mannitol phosphotransferase system of Escherichia coli. Kinetic evidence that the E. coli mannitol transport protein is a functional dimer.

2. Intramolecular distances within the Ca2+-ATPase from sarcoplasmic reticulum as estimated through fluorescence energy transfer between probes

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