Mercurials selectively inhibited Escherichia coli 414 ATPase (EC 3.6.1.3). Inhibition of the soluble ATPase (BF1) was greater than for the membrane-bound enzyme. The titration of 4 SH groups per mol BF1 with 0.05 mm-p-chloromercuri[14C]benzoate showed a good dose-response curve for the inhibition of basal ATPase but not for the trypsin-stimulated activity. Accessible SH groups did not seem to be related to the active site of the enzyme. Mercurials appeared to affect E. coli ATPase by inducing a molecular change in the holo-enzyme, followed by dissociation. One to two SH groups with different degrees of accessibility were located in the α and γ subunits of ATPase (BF1) but only one was located in the β subunit, irrespective of the concentration of p-chloromercuribenzoic acid, suggesting a structural role for SH groups in BF1.
AndreuJ. M.,
MuñozE.1975; Micrococcus lysodeikticus ATPase. Purification by preparative gel electrophoresis and subunit structure studied by urea and sodium dodecylsulfate gel electrophoresis. Biochimica et biophysica acta 387:228–233
AndreuJ. M.,
AlbendeaJ. A.,
MuñozE.1973; Membrane adenosine triphosphatase of Micrococcus lysodeikticus Molecular properties of the purified enzyme unstimulated by trypsin. European Journal of Biochemistry 37:505–515
AzocarO.,
MuñozE.1976; Molecular organization in bacterial cell membranes. Sulphydryl groups and disulfide bridges in Streptomyces albus and Escherichia colik12 cytoplasmic membranes. European Journal of Biochemistry 68:245–254
AzocarO.,
MuñozE.1977; Extrinsic and intrinsic factors that influence inactivation and purification of the unstable adenosine triphosphatase solubilized from membranes of an Escherichia coli k12 strain. Biochimica et biophysica acta 482:438–452
BairdB. A.,
HammesG. G.1977; Chemical cross-linking studies of beef heart mitochondrial coupling factor 1. Journal of Biological Chemistry 252:4743–4748
BrayG. A.1960; A simple efficient liquid scintillator for counting aqueous solutions in a liquid scintillation counter. Analytical Biochemistry 1:279–285
CarreiraJ.,
MuñozE.1975; Membrane bound and soluble adenosine triphosphatase of Escherichia colik12. Kinetic properties of the basal and trypsin-stimulated activities. Molecular and Cellular Biochemistry 9:85–95
CarreiraJ.,
LealJ. A.,
RojasM.,
MuñozE.1973; Membrane ATPase of Escherichia colik12. Selective solubilization of the enzyme and its stimulation by trypsin in the soluble and membrane-bound states. Biochimica et biophysica acta 307:541–556
CarreiraJ.,
AndreuJ. M.,
NietoM.,
MuñozE.1976; Membrane adenosine triphosphatase of Micrococcus lysodeikticus Isolation of two forms of the enzyme complex and correlation between enzymatic stability, latency and activity. Molecular and Cellular Biochemistry 10:67–76
CarreiraJ.,
AndreuJ. M.,
MuñozE.1977; Differential sensitivity to trypsin digestion of purified forms of Micrococcus lysodeikticus ATPase (BF1). A study of their structural and conformational differences and mechanism of conversion. Biochimica et biophysica acta 492:387–398
CoraoM. de,
SerranoJ. A.,
LealJ. A.,
PuigJ.,
MuñozE.1974; Isolation of murein-free spheroplast ‘ghosts’ from a strain of Escherichia colik12. Microbiologia espanola 27:283–298
EvansD. J.Jr1969; Membrane adenosine triphosphatase of Escherichia coli: activation by calcium ions and inhibition by monovalent cations. Journal of Bacteriology 100:914–922
FarronF.,
RackerE.1970; Studies on the mechanism of the conversion of coupling factor 1 from chloroplasts to an active adenosine triphosphatase. Biochemistry 9:3829–3836
GuntherT.,
PellnitzW.,
MarisG.1974; Effect of salts on the activity and inhibition of E. coli membrane ATPase by ethacrynic acid and inhibitors. Zeitschrift für Naturforschung 29:54–59
KobayashiH.,
AnrakuY.1972; Membrane-bound adenosine triphosphatase of Escherichia coli I. Partial purification and properties. Journal of Biochemistry 71:387–399
MuñozE.,
SaltonM. R. J.,
NgM. H.,
SchorM. T.1969; Membrane adenosine triphosphatase of Micrococcus lysodeikticus Purification, properties of the ‘soluble’ enzyme and properties of the membrane-bound enzyme. European Journal of Biochemistry 7:490–501
NelsonN.,
KannerB. I.,
GutnickD. L.1974; Purification and properties of Mg+2-Ca2+ adenosine triphosphatase from Escherichia coli
. Proceedings of the National Academy of Sciences of the United States of America712720–2724
PedersenP. L.1976; Adenosine triphosphatase from rat liver mitochondria. Evidence for a mercurial-sensitive site for the activating anion bicarbonate. Biochemical and Biophysical Research Communications 71:1182–1188
SeniorA. E.1975; Relationship of cysteine and tyrosine residues to adenosine triphosphate hydrolysis by mitochondrial adenosine triphosphatase. Biochemistry 12:3622–3627