A hybrid adenosine triphosphatase composed of F1 of Escherichia coli and F0 of Propionigenium modestum is a functional sodium ion pump

Biochemistry ◽  
1990 ◽  
Vol 29 (23) ◽  
pp. 5458-5463 ◽  
Author(s):  
Werner Laubinger ◽  
Gabriele Deckers-Hebestreit ◽  
Karlheinz Altendorf ◽  
Peter Dimroth
Keyword(s):  
Escherichia Coli ◽  
Adenosine Triphosphatase ◽  
Sodium Ion ◽  
Ion Pump ◽  
Propionigenium Modestum

Genetics of the Adenosine Triphosphatase Complex of Escherichia coli

1982 ◽  
pp. 453-457
Author(s):  
J. Allan Downie ◽  
Frank Gibson ◽  
Graeme B. Cox
Keyword(s):  
Escherichia Coli ◽  
Adenosine Triphosphatase

Transient Resonance Raman Spectroscopy of a Light-Driven Sodium-Ion-Pump Rhodopsin from Indibacter alkaliphilus

2017 ◽  
Vol 121 (17) ◽  
pp. 4431-4437 ◽  
Author(s):  
Kousuke Kajimoto ◽  
Takashi Kikukawa ◽  
Hiroki Nakashima ◽  
Haruki Yamaryo ◽  
Yuta Saito ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Sodium Ion ◽  
Ion Pump ◽  
Transient Resonance

scholarly journals A mutation affecting a second component of the F0 portion of the magnesium ion-stimulated adenosine triphosphatase of Escherichia coli K12. The uncC424 allele

1977 ◽  
Vol 164 (1) ◽  
pp. 193-198 ◽  
Author(s):  
F Gibson ◽  
G B Cox ◽  
J A Downie ◽  
J Radik
Keyword(s):  
Escherichia Coli ◽  
Electron Transport ◽  
Fluorescence Quenching ◽  
Mutant Strain ◽  
Mutant Allele ◽  
Adenosine Triphosphatase ◽  
Magnesium Ion ◽  
New Mutation ◽  
Similar Phenotype

A new mutant strain of Escherichia coli in which phosphorylation is uncoupled from electron transport was isolated. The new mutant strain has a similar phenotype to the uncB mutant described previously; results from reconstitution experiments in vitro indicate that the new mutation also affects a component of the F0 portion of the Mg2+-stimulated adenosine triphosphatase. A method was developed to incorporate mutant unc alleles into plasmids. Partial diploid strains were prepared in which the uncB402 allele was incorporated into the plasmid and the new unc mutation into the chromosome, or vice versa. Complementation between the mutant unc alleles was indicated by growth on succinate, growth yields on glucose, ATP-dependent transhydrogenase activities, ATP-induced atebrin-fluorescence quenching and oxidative-phosphorylation measurements. The gene in which the new mutation occurs is therefore distinct from the uncB gene, and the mutant allele was designated uncC424.

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