Self-avoiding tethered membranes

1989 ◽  
Vol 63 (12) ◽  
pp. 1324-1324 ◽  
Author(s):  
J.-S. Ho ◽  
A. Baumgärtner
Keyword(s):  
1992 ◽  
Vol 2 (5) ◽  
pp. 663-676 ◽  
Author(s):  
G. Gompper ◽  
D. M. Kroll
Keyword(s):  

Methods ◽  
2006 ◽  
Vol 39 (2) ◽  
pp. 134-146 ◽  
Author(s):  
Birgit Wiltschi ◽  
Wolfgang Knoll ◽  
Eva-Kathrin Sinner

1992 ◽  
Vol 46 (4) ◽  
pp. 1751-1768 ◽  
Author(s):  
David C. Morse ◽  
T. C. Lubensky
Keyword(s):  

1992 ◽  
Vol 45 (4) ◽  
pp. R2151-R2154 ◽  
Author(s):  
D. C. Morse ◽  
T. C. Lubensky ◽  
G. S. Grest

2009 ◽  
Vol 168 (1) ◽  
pp. 190-199 ◽  
Author(s):  
Minsub Chung ◽  
Randall D. Lowe ◽  
Yee-Hung M. Chan ◽  
Prasad V. Ganesan ◽  
Steven G. Boxer

1998 ◽  
Vol 95 (2) ◽  
pp. 137-140 ◽  
Author(s):  
FARID F. ABRAHAM
Keyword(s):  

2008 ◽  
Vol 417 (2) ◽  
pp. 555-560 ◽  
Author(s):  
Sophie A. Weiss ◽  
Richard J. Bushby ◽  
Stephen D. Evans ◽  
Peter J. F. Henderson ◽  
Lars J. C. Jeuken

We have developed a simple native-like surface-tethered membrane system to investigate the activity of cbo3 (cytochrome bo3), a terminal oxidase in Escherichia coli. The tethered membranes consist of E. coli inner-membrane extracts mixed with additional E. coli lipids containing various amounts of the cbo3 substrate UQ-10 (ubiquinol-10). Tethered membranes are formed by self-assembly from vesicles on to gold electrodes functionalized with cholesterol derivatives. cbo3 activity was monitored using CV (cyclic voltammetry) with electron transfer to cbo3 mediated by UQ-10. The apparent Km for oxygen with this system is 1.1±0.4 μM, in good agreement with values reported in the literature for whole-cell experiments and for purified cbo3. Increasing the concentration of lipophilic UQ-10 in the membrane leads to an increase in cbo3 activity. The activity of cbo3 with long-chain ubiquinones appears to be different from previous reports using short-chain substrate analogues such as UQ-1 in that typical Michaelis–Menten kinetics are not observed using UQ-10. This native-like membrane model thus provides new insights into the interaction of transmembrane enzymes with hydrophobic substrates which contrasts with studies using hydrophilic UQ analogues.


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