scholarly journals Effects of organic solvents and orthophosphate on the ATPase activity of F1 ATPase

FEBS Letters ◽  
1987 ◽  
Vol 213 (2) ◽  
pp. 333-336 ◽  
Author(s):  
Leopoldo de Meis
Keyword(s):  
Atpase Activity ◽  
Organic Solvents ◽  
F1 Atpase

Effect of Urea and Organic Solvents on the Mitochondrial F1 ATPase

1989 ◽  
Vol 44 (8) ◽  
pp. 955-958 ◽  
Author(s):  
George Dreyfus ◽  
Leopoldo de Meis
Keyword(s):  
Low Temperature ◽  
Protective Effect ◽  
Dimethyl Sulfoxide ◽  
Organic Solvents ◽  
Assay Medium ◽  
F1 Atpase ◽  
Cold Inactivation ◽  
Different Tissues

Mitochondrial F1 ATPase is inactivated by urea. Protection against urea inactivation is obtained when betaine, a methylamine found in different tissues, is added to the assay medium. Protection is also obtained upon the addition of either glycerol or dimethyl sulfoxide to the assay medium. The F, ATPase is rapidly inactivated at 4 °C. Inactivation by low temperature is prevented by betaine, glycerol and dimethyl sulfoxide. The protective effect of organic solvents and betaine against cold inactivation is prevented by urea.

scholarly journals Stimulation of F1-ATPase activity by sodium dodecyl sulfate

2010 ◽  
Vol 1797 (4) ◽  
pp. 435-442 ◽  
Author(s):  
Mohammad Delawar Hossain ◽  
Shou Furuike ◽  
Yasuhiro Onoue ◽  
Kengo Adachi ◽  
Masasuke Yoshida ◽  
...  
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Atpase Activity ◽  
Sodium Dodecyl ◽  
F1 Atpase ◽  
Dodecyl Sulfate ◽  
Stimulation Of

scholarly journals Stimulation of Cell Surface F1-ATPase Activity by Apolipoprotein A-I Inhibits Endothelial Cell Apoptosis and Promotes Proliferation

2009 ◽  
Vol 29 (7) ◽  
pp. 1125-1130 ◽  
Author(s):  
Claudia Radojkovic ◽  
Annelise Genoux ◽  
Véronique Pons ◽  
Guillaume Combes ◽  
Hugo de Jonge ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Cell Surface ◽  
Atpase Activity ◽  
Cell Apoptosis ◽  
Endothelial Cell Apoptosis ◽  
F1 Atpase ◽  
Apolipoprotein A ◽  
Stimulation Of

scholarly journals Modification of the mitochondrial F1-ATPase ∊ subunit, enhancement of the ATPase activity of the IF1–F1 complex and IF1-binding dependence of the conformation of the ∊ subunit

1997 ◽  
Vol 327 (2) ◽  
pp. 443-448 ◽  
Author(s):  
Giancarlo SOLAINI ◽  
Alessandra BARACCA ◽  
Edi GABELLIERI ◽  
Giorgio LENAZ
Keyword(s):  
Atpase Activity ◽  
Decay Rate ◽  
Atp Synthase ◽  
Hydrolytic Activity ◽  
Inhibitory Protein ◽  
Atpase Subunit ◽  
F1 Atpase ◽  
Phosphorescence Decay ◽  
Mitochondrial Atp Synthase ◽  
Significant Difference

Treatment of bovine heart submitochondrial particles with a low concentration of 2-hydroxy-5-nitrobenzyl bromide (HNB), a selective reagent for the Trp residue of the ε subunit [Baracca, Barogi, Lenaz and Solaini (1993) Int. J. Biochem. 25, 1269-1275], enhances the ATP hydrolytic activity of the particles exclusively when the natural inhibitor protein IF1 is present. Similarly, isolated F1 [the catalytic sector of the mitochondrial H+-ATPase complex (ATP synthase)] treated with the reagent has the ATPase activity enhanced exclusively if IF1 is bound to it. These experiments suggest that the modification of the ε subunit decreases the inhibitory activity of IF1, eliciting the search for a relationship between the ε subunit and the inhibitory protein. Certainly, a reverse relationship exists because HNB binds covalently to the isolated F1 exclusively when the inhibitory protein is present. This finding is consistent with the existence of the ε subunit in different conformational states depending on whether IF1 is bound to F1 or not. Support for this assertion is obtained by measurements of the intrinsic phosphorescence decay rate of F1, a probe of the Trp ε subunit conformation in situ [Solaini, Baracca, Parenti-Castelli and Strambini (1993) Eur. J. Biochem. 214, 729-734]. A significant difference in phosphorescence decay rate is detected when IF1 is added to preparations of F1 previously devoid of the inhibitory protein. These studies indicate that IF1 and the ε subunit of the mitochondrial F1-ATPase complex are related, suggesting a possible role of the ε subunit in the mechanism of regulation of the mitochondrial ATP synthase.

scholarly journals Oxidative phosphorylation by mutant Escherichia coli membranes with impaired proton permeability

1983 ◽  
Vol 216 (1) ◽  
pp. 143-150 ◽  
Author(s):  
G B Cox ◽  
D A Jans ◽  
F Gibson ◽  
L Langman ◽  
A E Senior ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Oxidative Phosphorylation ◽  
Atpase Activity ◽  
Gene Dosage ◽  
Control Strain ◽  
Proton Permeability ◽  
F1f0 Atpase ◽  
F1 Atpase ◽  
C Subunit

The effect on the function of the Escherichia coli F1F0-ATPase of the substitution of leucine-31 by phenylalanine in the c-subunit of the enzyme was examined. The assembly of the mutant c-subunit requires an increased gene dosage [Jans, Fimmel, Langman, James, Downie, Senior, Ash, Gibson & Cox (1983) Biochem. J. 211, 717-726], and this was achieved by incorporation of the uncE408 or uncE463 alleles on to F-plasmids or multicopy plasmids. Membranes from strains carrying either the uncE463 or uncE408 alleles on F-plasmids or multicopy plasmids were capable of carrying out oxidative phosphorylation. In particular, membranes from strain AN1928 (pAN162, uncE463) gave phosphorylation rates and P/O ratios equal to or greater than those obtained for the control strain AN1460 (pAN45, unc+). However, the mutant membranes, on removal of the F1-ATPase, appeared to be proton-impermeable. The ATPase activity of the mutant membranes was also resistant to the inhibitor dicyclohexylcarbodi-imide.

Monoclonal antibody modification of the ATPase activity of Escherichia coli F1 ATPase

Biochemistry ◽  
1990 ◽  
Vol 29 (45) ◽  
pp. 10387-10393 ◽  
Author(s):  
Robert Aggeler ◽  
Janet Mendel-Hartvig ◽  
Roderick A. Capaldi
Keyword(s):  
Escherichia Coli ◽  
Monoclonal Antibody ◽  
Atpase Activity ◽  
F1 Atpase

scholarly journals The F1F0-ATPase of Escherichia coli. Substitution of proline by leucine at position 64 in the c-subunit causes loss of oxidative phosphorylation

1983 ◽  
Vol 213 (2) ◽  
pp. 451-458 ◽  
Author(s):  
A L Fimmel ◽  
D A Jans ◽  
L Langman ◽  
L B James ◽  
G R Ash ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Fluorescence Quenching ◽  
Oxidative Phosphorylation ◽  
Atpase Activity ◽  
Base Change ◽  
Helix Axis ◽  
F1f0 Atpase ◽  
F1 Atpase ◽  
C Subunit

The uncE410 allele differs from the normal uncE gene in that C leads to T base changes occur at nucleotides 190 and 191, resulting in proline at position 64 in the c-subunit of the F1F0-ATPase being replaced by leucine. Two partial-revertant strains were isolated in which alanine-20 of the c-subunit was replaced by proline, owing to a G leads to C base change at nucleotide 58. These c-subunits, coded for by the uncE501 and uncE502 alleles, therefore contained two amino acid changes, namely proline-64 leads to leucine, and alanine-20 leads to proline. Membranes prepared from the partial-revertant strains lacked ATP-dependent atebrin-fluorescence-quenching activity but were able to carry out oxidative phosphorylation. The ATPase activity of the F1-ATPase was inhibited when bound to membranes from strains carrying the uncE410, uncE501 and uncE502 alleles. It is concluded that a bend in the helix axis in one of the arms of the c-subunit hairpin structure is required for integration of the c-subunit into a functional F1F0-ATPase.

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