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Pre‐steady state kinetics of nucleotide‐triphosphate hydrolysis by mitochondrial F 1 ‐ATPase from yeast
Author(s) -
Recktenwald Diether,
Hess Benno
Publication year - 1979
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(79)81223-5
Subject(s) - citation , physics , chemistry , combinatorics , library science , computer science , mathematics
In [l] we described the observation of a timedelayed onset of F,-ATPase activity of yeast (YFr) which indicated a conformational transition of the enzyme complex by a substrate-triggered activation mechanism. This observation was later confirmed for Fr-ATPase from Neurospora as well as thermophilic bacteria (TF,) [2] and by others for the case of Fr -ATPase of beef-heart [3] and chloroplast [4]. In a search for the mechanism of this conformation change we recently analyzed the sensitivity of the lag time toward nucleotide triphosphates, ADP, pH and anions, and observed only a sensitivity toward ADP. The results of these experiments are reported here.