Premium
Steady‐state kinetics of F 1 ‐ATPase
Author(s) -
Roveri Oscar A.,
Calcaterra Nora B.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80056-9
Subject(s) - kinetics , bicarbonate , chemistry , atpase , enzyme , enzyme kinetics , steady state (chemistry) , medicinal chemistry , biophysics , biochemistry , active site , biology , organic chemistry , physics , quantum mechanics
The kinetic behaviour of the ATPase activity of beef heart F 1 depends largely on the exposure of the enzyme to some anionic ligands such as sulphate and/or EDTA. F 1 prepared in the presence of such anions exhibited a triphasic kinetic pattern whereas F 1 from which those anions were removed by dialysis exhibited only two K m values for ATP. Conversely to what has been previously reported, bicarbonate did not linearize F 2 ‐ATPase kinetics. Moreover, anion activation cannot be simply explained by promotion of ADP release but mainly by an increase in affinity of the third catalytic site for ATP.