Effects of Aeration during Growth of Bacillus stearothermophilus; on Proton Pumping Activity and Change of TerminalOxidases1

1991 ◽  
Vol 110 (6) ◽  
pp. 1016-1021 ◽  
Author(s):  
Nobuhito Sone ◽  
Yoshihisa Fujiwara
Keyword(s):  
Bacillus Stearothermophilus ◽  
Proton Pumping ◽  
Pumping Activity

Chemical Modification of the Bovine Mitochondrialbc1Complex Reveals Critical Acidic Residues Involved in the Proton Pumping Activity†

Biochemistry ◽  
1998 ◽  
Vol 37 (7) ◽  
pp. 2037-2043 ◽  
Author(s):  
Tiziana Cocco ◽  
Marco Di Paola ◽  
Sergio Papa ◽  
Michele Lorusso
Keyword(s):  
Chemical Modification ◽  
Proton Pumping ◽  
Acidic Residues ◽  
Pumping Activity

Reconstitution of proton pumping activity of a plasma membrane ATPase purified from radish

1985 ◽  
Vol 37 (3) ◽  
pp. 189-193 ◽  
Author(s):  
Maria Cecilia Cocucci ◽  
Maria Ida De Michelis ◽  
Maria Chiara Pugliarello ◽  
Franca Rasi-Caldogno
Keyword(s):  
Plasma Membrane ◽  
Proton Pumping ◽  
Plasma Membrane Atpase ◽  
Membrane Atpase ◽  
Pumping Activity

scholarly journals Eisosomes are metabolically regulated storage compartments for APC-type nutrient transporters

2018 ◽  
Vol 29 (17) ◽  
pp. 2113-2127 ◽  
Author(s):  
Akshay Moharir ◽  
Lincoln Gay ◽  
Daniel Appadurai ◽  
James Keener ◽  
Markus Babst
Keyword(s):  
Plasma Membrane ◽  
Cell Surface ◽  
Proton Pumping ◽  
Proton Gradient ◽  
Lipid Domains ◽  
Nutrient Transporters ◽  
Major Function ◽  
Show Evidence ◽  
Higher Eukaryotes ◽  
Pumping Activity

Eisosomes are lipid domains of the yeast plasma membrane that share similarities to caveolae of higher eukaryotes. Eisosomes harbor APC-type nutrient transporters for reasons that are poorly understood. Our analyses support the model that eisosomes function as storage compartments, keeping APC transporters in a stable, inactive state. By regulating eisosomes, yeast is able to balance the number of proton-driven APC transporters with the proton-pumping activity of Pma1, thereby maintaining the plasma membrane proton gradient. Environmental or metabolic changes that disrupt the proton gradient cause the rapid restructuring of eisosomes and results in the removal of the APC transporters from the cell surface. Furthermore, we show evidence that eisosomes require the presence of APC transporters, suggesting that regulating activity of nutrient transporters is a major function of eisosomes.

scholarly journals Susceptibility of the Formate Hydrogenlyase Reaction to the Protonophore CCCP Depends on the Total Hydrogenase Composition

Inorganics ◽  
2020 ◽  
Vol 8 (6) ◽  
pp. 38
Author(s):  
Janik Telleria Marloth ◽  
Constanze Pinske
Keyword(s):  
Complex I ◽  
H2 Production ◽  
Proton Pumping ◽  
Fermentative Hydrogen Production ◽  
Iron Sulfur ◽  
Formate Hydrogenlyase ◽  
Respiratory Complex I ◽  
Fermentative Hydrogen ◽  
Pumping Activity ◽  
Higher Sensitivity

Fermentative hydrogen production by enterobacteria derives from the activity of the formate hydrogenlyase (FHL) complex, which couples formate oxidation to H2 production. The molybdenum-containing formate dehydrogenase and type-4 [NiFe]-hydrogenase together with three iron-sulfur proteins form the soluble domain, which is attached to the membrane by two integral membrane subunits. The FHL complex is phylogenetically related to respiratory complex I, and it is suspected that it has a role in energy conservation similar to the proton-pumping activity of complex I. We monitored the H2-producing activity of FHL in the presence of different concentrations of the protonophore CCCP. We found an inhibition with an apparent EC50 of 31 µM CCCP in the presence of glucose, a higher tolerance towards CCCP when only the oxidizing hydrogenase Hyd-1 was present, but a higher sensitivity when only Hyd-2 was present. The presence of 200 mM monovalent cations reduced the FHL activity by more than 20%. The Na+/H+ antiporter inhibitor 5-(N-ethyl-N-isopropyl)-amiloride (EIPA) combined with CCCP completely inhibited H2 production. These results indicate a coupling not only between Na+ transport activity and H2 production activity, but also between the FHL reaction, proton import and cation export.

Chemical modification of the CuA site affects the proton pumping activity of cytochrome c oxidase

Biochemistry ◽  
1988 ◽  
Vol 27 (1) ◽  
pp. 296-301 ◽  
Author(s):  
Thomas Nilsson ◽  
Jeff Gelles ◽  
Peter Mark Li ◽  
Sunney I. Chan
Keyword(s):  
Cytochrome C ◽  
Chemical Modification ◽  
Cytochrome C Oxidase ◽  
Proton Pumping ◽  
Pumping Activity

scholarly journals Liposome Model Systems to Study the Endosomal Escape of Cell-Penetrating Peptides: Transport across Phospholipid Membranes Induced by a Proton Gradient

2011 ◽  
Vol 2011 ◽  
pp. 1-7 ◽  
Author(s):  
Fatemeh Madani ◽  
Alex Perálvarez-Marín ◽  
Astrid Gräslund
Keyword(s):  
Cell Penetrating Peptides ◽  
Proton Pumping ◽  
Model Systems ◽  
Endosomal Escape ◽  
Vesicle Membrane ◽  
Large Unilamellar Vesicles ◽  
Octyl Glucoside ◽  
Cell Penetrating ◽  
Pumping Activity ◽  
Extrusion Method

Detergent-mediated reconstitution of bacteriorhodopsin (BR) into large unilamellar vesicles (LUVs) was investigated, and the effects were carefully characterized for every step of the procedure. LUVs were prepared by the extrusion method, and their size and stability were examined by dynamic light scattering. BR was incorporated into the LUVs using the detergent-mediated reconstitution method and octyl glucoside (OG) as detergent. The result of measuring pH outside the LUVs suggested that in the presence of light, BR pumps protons from the outside to the inside of the LUVs, creating acidic pH inside the vesicles. LUVs with 20% negatively charged headgroups were used to model endosomes with BR incorporated into the membrane. The fluorescein-labeled cell-penetrating peptide penetratin was entrapped inside these BR-containing LUVs. The light-induced proton pumping activity of BR has allowed us to observe the translocation of fluorescein-labeled penetratin across the vesicle membrane.

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