Tight divalent metal binding to Escherichia coli F1-adenosinetriphosphatase. Complete substitution of intrinsic magnesium by manganese or cobalt and studies of metal binding sites

Tight divalent metal binding sites in Escherichia coli F1-adenosinetriphosphatase (F1-ATPase) were studied. Native enzyme contained two Mg per F1, confirming previous results. All of the Mg may be replaced by Co or Mn using a dissociation-repolymerization procedure. The substituted enzymes are homog...

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Veröffentlicht in:	Biochemistry (Easton) 1985-07, Vol.24 (16), p.4490-4494
Hauptverfasser:	Smith, Richard A, Latchney, Lisa R, Senior, Alan E
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Binding Sites Biological and medical sciences Cobalt - metabolism Dicyclohexylcarbodiimide - pharmacology Enzymes and enzyme inhibitors Escherichia coli - enzymology Fundamental and applied biological sciences. Psychology Hydrolases Macromolecular Substances Magnesium - metabolism Manganese - metabolism Proton-Translocating ATPases - antagonists & inhibitors Proton-Translocating ATPases - metabolism
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