Rotational Mobility of Membrane-Bound Cytochrome o of Escherichia coli and Cytochrome a1 of Thiobacillus ferro-oxidans

1979 ◽  
Vol 7 (5) ◽  
pp. 1112-1114 ◽  
Author(s):  
PETER B. GARLAND ◽  
MICHAEL T. DAVISON ◽  
CHRISTOPHER H. MOORE
Keyword(s):  
Escherichia Coli ◽  
Rotational Mobility ◽  
Cytochrome O ◽  
Membrane Bound

Relationships between membrane-bound cytochrome o from Vitreoscilla and that of Escherichia coli

1988 ◽  
Vol 933 (1) ◽  
pp. 179-183 ◽  
Author(s):  
Christos D. Georgiou ◽  
Peter Cokic ◽  
Kimberly Carter ◽  
Dale A. Webster ◽  
Robert B. Gennis
Keyword(s):  
Escherichia Coli ◽  
Cytochrome O ◽  
Membrane Bound

scholarly journals Kinetic characterization of the membrane-bound cytochromes of Escherichia coli grown under a variety of conditions by using a stopped-flow dual-wavelength spectrophotometer

1976 ◽  
Vol 154 (2) ◽  
pp. 285-294 ◽  
Author(s):  
B A. Haddock ◽  
J. A Downie ◽  
P B. Garland
Keyword(s):  
Escherichia Coli ◽  
Oxidation Kinetics ◽  
Difference Spectrum ◽  
Stopped Flow ◽  
Oxidation Rates ◽  
Cytochrome O ◽  
Membrane Bound ◽  
Cytochrome D ◽  
Kinetics Of

A study was made of the rapid oxidation kinetics of the cytochromes of Escherichia coli. The b-type cytochromes were kinetically heterogeneous, with one species (presumably cytochrome o) oxidized so rapidly that it could fully support observed oxidation rates. Cytochrome d but not cytochrome a1 was also kinetically competent to support respiration. However, in cells grown anaerobically in the presence of NO3-, cytochrome d exhibited slow oxidation kinetics and a red-shift in its reduced-minus-oxidized difference spectrum.

scholarly journals Improving cell-free glycoprotein synthesis by characterizing and enriching native membrane vesicles

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Jasmine M. Hershewe ◽  
Katherine F. Warfel ◽  
Shaelyn M. Iyer ◽  
Justin A. Peruzzi ◽  
Claretta J. Sullivan ◽  
...  
Keyword(s):  
Gene Expression ◽  
Escherichia Coli ◽  
Synthetic Biology ◽  
Membrane Protein ◽  
Membrane Vesicles ◽  
Processing Methods ◽  
Glycoprotein Synthesis ◽  
On Demand ◽  
Free Gene ◽  
Membrane Bound

AbstractCell-free gene expression (CFE) systems from crude cellular extracts have attracted much attention for biomanufacturing and synthetic biology. However, activating membrane-dependent functionality of cell-derived vesicles in bacterial CFE systems has been limited. Here, we address this limitation by characterizing native membrane vesicles in Escherichia coli-based CFE extracts and describing methods to enrich vesicles with heterologous, membrane-bound machinery. As a model, we focus on bacterial glycoengineering. We first use multiple, orthogonal techniques to characterize vesicles and show how extract processing methods can be used to increase concentrations of membrane vesicles in CFE systems. Then, we show that extracts enriched in vesicle number also display enhanced concentrations of heterologous membrane protein cargo. Finally, we apply our methods to enrich membrane-bound oligosaccharyltransferases and lipid-linked oligosaccharides for improving cell-free N-linked and O-linked glycoprotein synthesis. We anticipate that these methods will facilitate on-demand glycoprotein production and enable new CFE systems with membrane-associated activities.

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